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Volumn 4, Issue 11, 1996, Pages 1263-1275

The structure of the C-terminal domain of methionine synthase: Presenting S-adenosylmethionine for reductive methylation of B12

Author keywords

adenosylmethionine; B12; cobalamin; methionine synthase

Indexed keywords

ESCHERICHIA COLI; MAMMALIA;

EID: 0030589146     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00135-9     Document Type: Article
Times cited : (112)

References (85)
  • 1
    • 0037832819 scopus 로고
    • 12-dependent methionine biosynthesis
    • Dolphin, D., ed John Wiley & Sons, New York
    • 12. (Dolphin, D., ed), pp. 307-355, John Wiley & Sons, New York.
    • (1982) 12 , pp. 307-355
    • Taylor, R.T.1
  • 2
    • 0037905417 scopus 로고
    • Methionine synthetase: Characterization of protein components and mechanisms for activation and catalysis
    • Yagi, K., ed Scientific Societies Press, Tokyo, Japan
    • Fujii, K. & Huennekens, F.M. (1979). Methionine synthetase: characterization of protein components and mechanisms for activation and catalysis. In Biochemical Aspects of Nutrition. (Yagi, K., ed), pp. 173-183, Scientific Societies Press, Tokyo, Japan.
    • (1979) Biochemical Aspects of Nutrition , pp. 173-183
    • Fujii, K.1    Huennekens, F.M.2
  • 3
    • 0025697224 scopus 로고
    • Participation of cob(l)alamin in the reaction catalyzed by methionine synthase from Escherichia coli: A steady-state and rapid reaction kinetic analysis
    • Banerjee, R.V., Frasca, V., Ballou, D.P. & Matthews, R.G. (1990). Participation of cob(l)alamin in the reaction catalyzed by methionine synthase from Escherichia coli: a steady-state and rapid reaction kinetic analysis. Biochemistry 29, 11101-11109.
    • (1990) Biochemistry , vol.29 , pp. 11101-11109
    • Banerjee, R.V.1    Frasca, V.2    Ballou, D.P.3    Matthews, R.G.4
  • 4
    • 0008336988 scopus 로고
    • Cofactor requirements and intermediates in methionine biosynthesis
    • Mangum, J.H. & Scrimgeour, K.C. (1962). Cofactor requirements and intermediates in methionine biosynthesis. Feder. Proc. 21, 242.
    • (1962) Feder. Proc. , vol.21 , pp. 242
    • Mangum, J.H.1    Scrimgeour, K.C.2
  • 5
    • 0001877313 scopus 로고
    • Cobalamin and the synthesis of methionine by Escherichia coli
    • Foster, M.A, Dilworth, M.J. & Woods, D.D. (1964). Cobalamin and the synthesis of methionine by Escherichia coli. Nature 201, 39-42.
    • (1964) Nature , vol.201 , pp. 39-42
    • Foster, M.A.1    Dilworth, M.J.2    Woods, D.D.3
  • 6
    • 0016173119 scopus 로고
    • Activation of methionine synthetase by a reduced triphosphopyridine nucleotide-dependent flavoprotein system
    • Fujii, K. & Huennekens, F.M. (1974). Activation of methionine synthetase by a reduced triphosphopyridine nucleotide-dependent flavoprotein system. J. Biol. Chem. 249, 6745-6753.
    • (1974) J. Biol. Chem. , vol.249 , pp. 6745-6753
    • Fujii, K.1    Huennekens, F.M.2
  • 7
    • 0025023541 scopus 로고
    • Mechanism of reductive activation of cobalamin-dependent methionine synthase: An electron paramagnetic resonance spectroelectrochemical study
    • Banerjee, R.V., Harder, S.R., Ragsdale, S.W. & Matthews, R.G. (1990). Mechanism of reductive activation of cobalamin-dependent methionine synthase: an electron paramagnetic resonance spectroelectrochemical study. Biochemistry 29, 1129-1135.
    • (1990) Biochemistry , vol.29 , pp. 1129-1135
    • Banerjee, R.V.1    Harder, S.R.2    Ragsdale, S.W.3    Matthews, R.G.4
  • 8
    • 0000300592 scopus 로고
    • Enzymatic synthesis of the methyl group of methionine. VII. Isolation of a cobalamin-containing transmethylase (5-methyltetrahydrofolatehomocysteine) from mammalian liver
    • Loughlin, R.E., Elford, H.L. & Buchanan, J.M. (1964). Enzymatic synthesis of the methyl group of methionine. VII. Isolation of a cobalamin-containing transmethylase (5-methyltetrahydrofolatehomocysteine) from mammalian liver. J. Biol. Chem. 239, 2888-2895.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2888-2895
    • Loughlin, R.E.1    Elford, H.L.2    Buchanan, J.M.3
  • 9
    • 0027986886 scopus 로고
    • Purification and kinetic mechanism of a mammalian methionine synthase from pig liver
    • Chen, Z., Crippen, K., Gulati, S., & Banerjee, R. (1994). Purification and kinetic mechanism of a mammalian methionine synthase from pig liver. J. Biol. Chem. 269, 27193-27197.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27193-27197
    • Chen, Z.1    Crippen, K.2    Gulati, S.3    Banerjee, R.4
  • 10
    • 33845376143 scopus 로고
    • Stereochemical analysis of the methyl transfer catalyzed by cobalamin-dependent methionine synthase from Escherichia coli. B
    • Zydowsky, T.M., et al., & Floss, H.G. (1986). Stereochemical analysis of the methyl transfer catalyzed by cobalamin-dependent methionine synthase from Escherichia coli. B. J. Am. Chem. Soc. 108, 3152-3153.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 3152-3153
    • Zydowsky, T.M.1    Floss, H.G.2
  • 11
    • 77956909555 scopus 로고
    • N5-methyltetrahydrofolatehomocysteine methyltransferases
    • Boyer, .D., ed Academic Press, New York
    • Taylor, R.T. & Weissbach, H. (1973). N5-methyltetrahydrofolatehomocysteine methyltransferases. In The Enzymes, Vol. IX. (Boyer, .D., ed), pp.121-165, Academic Press, New York.
    • (1973) The Enzymes , vol.9 , pp. 121-165
    • Taylor, R.T.1    Weissbach, H.2
  • 12
    • 0017626285 scopus 로고
    • Activation of methionine synthase: Further characterization of the flavoprotein system
    • Fujii, K., Galivan, J.H. & Huennekens, F.M. (1977). Activation of methionine synthase: further characterization of the flavoprotein system. Arch. Biochem. Biophys. 178, 662-670.
    • (1977) Arch. Biochem. Biophys. , vol.178 , pp. 662-670
    • Fujii, K.1    Galivan, J.H.2    Huennekens, F.M.3
  • 13
    • 0024364303 scopus 로고
    • Cloning and sequence analysis of the Escherichia coli metH gene encoding cobalamin-dependent methionine synthase and isolation of a tryptic fragment containing the cobalamin-binding domain
    • Banerjee, R.V, Johnston, N.L., Sobeski, J.K., Datta, P. & Matthews, R.G. (1989). Cloning and sequence analysis of the Escherichia coli metH gene encoding cobalamin-dependent methionine synthase and isolation of a tryptic fragment containing the cobalamin-binding domain. J. Biol. Chem. 264, 13888-13895.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13888-13895
    • Banerjee, R.V.1    Johnston, N.L.2    Sobeski, J.K.3    Datta, P.4    Matthews, R.G.5
  • 14
    • 0027445612 scopus 로고
    • Assignment of enzymatic function to specific protein regions of cobalamin-dependent methionine synthase from Escherichia coli
    • Drummond, J.T., Huang, S., Blumenthal, R.M. & Matthews, R.G. (1993). Assignment of enzymatic function to specific protein regions of cobalamin-dependent methionine synthase from Escherichia coli. Biochemistry 32, 9290-9295.
    • (1993) Biochemistry , vol.32 , pp. 9290-9295
    • Drummond, J.T.1    Huang, S.2    Blumenthal, R.M.3    Matthews, R.G.4
  • 15
    • 33748906122 scopus 로고    scopus 로고
    • Substrate reactivity is controlled by the N-terminal 71 kDa domain of E. coli methionine synthase
    • Goulding, C.W. & Matthews, R.G. (1996). Substrate reactivity is controlled by the N-terminal 71 kDa domain of E. coli methionine synthase. FASEB J. 10, A973.
    • (1996) FASEB J. , vol.10
    • Goulding, C.W.1    Matthews, R.G.2
  • 16
    • 0028075318 scopus 로고
    • 4folate:corrinoid/iron sulfur protein methyltransferase fromClostridiumthermoaceticum
    • 4folate:corrinoid/iron sulfur protein methyltransferase fromClostridiumthermoaceticum. J. Bacteriol. 176, 6127-6130.
    • (1994) J. Bacteriol. , vol.176 , pp. 6127-6130
    • Roberts, D.L.1    Zhao, S.2    Doukov, T.3    Ragsdale, S.W.4
  • 17
    • 0028769662 scopus 로고
    • How a protein binds B12: A 3.0 Å X-ray structure of the B12 binding domains of methionine synthase
    • Drennan, C.L., Huang, S., Drummond, J.T., Matthews, R. G.& Ludwig, M.L. (1994). How a protein binds B12: a 3.0 Å X-ray structure of the B12 binding domains of methionine synthase. Science 266, 1669-1674.
    • (1994) Science , vol.266 , pp. 1669-1674
    • Drennan, C.L.1    Huang, S.2    Drummond, J.T.3    Matthews, R.G.4    Ludwig, M.L.5
  • 18
    • 0026099830 scopus 로고
    • Isolation, cloning, mapping, and nucleotide sequencing of the gene encoding flavodoxin in Escherichia coli
    • Osborne, C., Chen, L.-M. & Matthews, R.G. (1991). Isolation, cloning, mapping, and nucleotide sequencing of the gene encoding flavodoxin in Escherichia coli. J. Bacteriol. 173, 1729-1737.
    • (1991) J. Bacteriol. , vol.173 , pp. 1729-1737
    • Osborne, C.1    Chen, L.-M.2    Matthews, R.G.3
  • 19
    • 16144365743 scopus 로고    scopus 로고
    • Interaction of E. coli cobalamin-dependent methionine synthase and its physiological partner flavodoxin: Binding of flavodoxin leads to axial ligand dissociation from the cobalamin cofactor
    • in press
    • Hoover, D.M., Jarrett, J.T., Sands, R.H., Dunham, W.R., Ludwig, M.L. & Matthews, R.G. (1996). Interaction of E. coli cobalamin-dependent methionine synthase and its physiological partner flavodoxin: Binding of flavodoxin leads to axial ligand dissociation from the cobalamin cofactor. Biochemistry, in press.
    • (1996) Biochemistry
    • Hoover, D.M.1    Jarrett, J.T.2    Sands, R.H.3    Dunham, W.R.4    Ludwig, M.L.5    Matthews, R.G.6
  • 21
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, RA & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Cryst. A 47, 392-400.
    • (1991) Acta Cryst. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 22
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • Connolly, M. (1983). Solvent-accessible surfaces of proteins and nucleic acids. Science 221, 709-713.
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.1
  • 23
    • 0023051843 scopus 로고
    • Internal cavities and buried waters in globular proteins
    • Rashin, A.A., lofin, M. & Honig, B. (1986). Internal cavities and buried waters in globular proteins. Biochemistry 25, 3619-3625.
    • (1986) Biochemistry , vol.25 , pp. 3619-3625
    • Rashin, A.A.1    Lofin, M.2    Honig, B.3
  • 24
    • 0017411710 scopus 로고
    • The Protein Data Bank: A computer-based archival file for macromolecular structures
    • Bernstein, F.C., et al., & Tasumi, M. (1977). The Protein Data Bank: a computer-based archival file for macromolecular structures. J. Mol. Biol. 112, 532-542.
    • (1977) J. Mol. Biol. , vol.112 , pp. 532-542
    • Bernstein, F.C.1    Tasumi, M.2
  • 25
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B.K. & Richards, F.M. (1971). The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55, 379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.K.1    Richards, F.M.2
  • 26
    • 0022798602 scopus 로고
    • Atomic size packing defects in proteins
    • Connolly, M. (1986). Atomic size packing defects in proteins. Int. J. Pept. Protein Res. 28, 360-363.
    • (1986) Int. J. Pept. Protein Res. , vol.28 , pp. 360-363
    • Connolly, M.1
  • 27
    • 0028607523 scopus 로고
    • Cavities and packing at protein interfaces
    • Hubbard, S.J. & Argos, P. (1994). Cavities and packing at protein interfaces. Protein Sci. 3, 2194-2206.
    • (1994) Protein Sci. , vol.3 , pp. 2194-2206
    • Hubbard, S.J.1    Argos, P.2
  • 28
    • 0028274954 scopus 로고
    • Intramolecular cavities in globular proteins
    • Hubbard, S.J., Gross, K.-H. & Argos, P. (1994). Intramolecular cavities in globular proteins. Protein Eng. 7, 613-626.
    • (1994) Protein Eng. , vol.7 , pp. 613-626
    • Hubbard, S.J.1    Gross, K.-H.2    Argos, P.3
  • 29
    • 0028095182 scopus 로고
    • Buried waters and internal cavities in monomeric proteins
    • Williams, M.A., Goodfellow, J.M. & Thornton, J.M. (1994). Buried waters and internal cavities in monomeric proteins. Protein Sci. 3, 1224-1235.
    • (1994) Protein Sci. , vol.3 , pp. 1224-1235
    • Williams, M.A.1    Goodfellow, J.M.2    Thornton, J.M.3
  • 30
    • 0028335096 scopus 로고
    • Structural mechanisms for domain movement in proteins
    • Gerstein, M., Lesk, A.M. & Chothia C. (1994). Structural mechanisms for domain movement in proteins. Biochemistry 33, 6739-6749.
    • (1994) Biochemistry , vol.33 , pp. 6739-6749
    • Gerstein, M.1    Lesk, A.M.2    Chothia, C.3
  • 31
    • 0028353469 scopus 로고
    • Nitrous oxide inactivation of cobalamin-dependent methionine synthase from Escherichia coli: Characterization of the damage to the enzyme and prosthetic group
    • Drummond, J.T. & Matthews, R.G. (1994). Nitrous oxide inactivation of cobalamin-dependent methionine synthase from Escherichia coli: characterization of the damage to the enzyme and prosthetic group. Biochemistry 33, 3742-3750.
    • (1994) Biochemistry , vol.33 , pp. 3742-3750
    • Drummond, J.T.1    Matthews, R.G.2
  • 32
    • 0016420033 scopus 로고
    • Mechanisms of protein and polypeptide helix initiation
    • Blagdon, D.E. & Goodman, M. (1975). Mechanisms of protein and polypeptide helix initiation. Biopolymers 14, 241-245.
    • (1975) Biopolymers , vol.14 , pp. 241-245
    • Blagdon, D.E.1    Goodman, M.2
  • 33
    • 0021892842 scopus 로고
    • The pKa values of two histidine residues in human haemoglobin, the Bohr effect, and the dipole moments of α helices
    • Perutz, M.F., Gronenborn, A.M., Clore, G.M., Fogg, J.H. & Shih, D.T.-B. (1985). The pKa values of two histidine residues in human haemoglobin, the Bohr effect, and the dipole moments of α helices. J.Mol. Biol. 183, 491-498.
    • (1985) J.Mol. Biol. , vol.183 , pp. 491-498
    • Perutz, M.F.1    Gronenborn, A.M.2    Clore, G.M.3    Fogg, J.H.4    Shih, D.T.-B.5
  • 34
    • 0023726958 scopus 로고
    • Stabilization of protein structure by interaction of α helix dipole with a charged side chain
    • Sali, D., Bycroft, M. & Fersht, A.R. (1988). Stabilization of protein structure by interaction of α helix dipole with a charged side chain. Nature 335, 740-743.
    • (1988) Nature , vol.335 , pp. 740-743
    • Sali, D.1    Bycroft, M.2    Fersht, A.R.3
  • 35
    • 0002460125 scopus 로고
    • Inhibitors of S-adenosylhomocysteine hydrolase and their role in the regulation of biological methylation
    • Usdin, E., Borchardt, R.T. & Creveling, C.R., eds Elsevier/North-Holland, New York
    • Cantoni, G.L., Richards, H.H. & Chiang, P.K. (1979). Inhibitors of S-adenosylhomocysteine hydrolase and their role in the regulation of biological methylation. In Transmethylation, (Usdin, E., Borchardt, R.T. & Creveling, C.R., eds), pp. 155-164, Elsevier/North-Holland, New York.
    • (1979) Transmethylation , pp. 155-164
    • Cantoni, G.L.1    Richards, H.H.2    Chiang, P.K.3
  • 36
    • 0028956315 scopus 로고
    • Universal catalytic domain structure of AdoMet-dependent methyltransferases
    • Schluckebier, G., O'Gara, M., Saenger, W. & Cheng, X. (1995). Universal catalytic domain structure of AdoMet-dependent methyltransferases. J. Mol. Biol. 247, 16-20.
    • (1995) J. Mol. Biol. , vol.247 , pp. 16-20
    • Schluckebier, G.1    O'Gara, M.2    Saenger, W.3    Cheng, X.4
  • 37
    • 0028841409 scopus 로고
    • Structure-guided analysis reveals nine sequence motifs conserved among DNA aminomethyltransferases, and suggests a catalytic mechanism for these enzymes
    • Malone, T., Blumenthal, R.M. & Cheng, X. (1995). Structure-guided analysis reveals nine sequence motifs conserved among DNA aminomethyltransferases, and suggests a catalytic mechanism for these enzymes. J. Mol. Biol. 253, 618-632.
    • (1995) J. Mol. Biol. , vol.253 , pp. 618-632
    • Malone, T.1    Blumenthal, R.M.2    Cheng, X.3
  • 38
    • 0024398664 scopus 로고
    • Sequence of the D-aspartyl/L-isoaspartyl protein methyltransferase from human erythrocytes. Common sequence motifs for protein, DNA, RNA and small molecule S-adenosylmethionine-dependent methyltransferases
    • Ingrosso, D., Fowler, A.V., Bleibaum, J. & Clarke, S. (1989). Sequence of the D-aspartyl/L-isoaspartyl protein methyltransferase from human erythrocytes. Common sequence motifs for protein, DNA, RNA and small molecule S-adenosylmethionine-dependent methyltransferases. J. Biol. Chem. 264, 20121-20139.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20121-20139
    • Ingrosso, D.1    Fowler, A.V.2    Bleibaum, J.3    Clarke, S.4
  • 39
    • 0027338134 scopus 로고
    • Crystal structure of the Hhal DNA methyltransferase complexed with S-adenosyl-L-methionine
    • Cheng, X, Kumar, S., Posfai, J., Pflugrath, J.W. & Roberts, R. J. (1993). Crystal structure of the Hhal DNA methyltransferase complexed with S-adenosyl-L-methionine. Cell 74, 299-307.
    • (1993) Cell , vol.74 , pp. 299-307
    • Cheng, X.1    Kumar, S.2    Posfai, J.3    Pflugrath, J.W.4    Roberts, R.J.5
  • 40
    • 0027946731 scopus 로고
    • Three-dimensional structure of the adenine-specific DNA methyltransferase M-Taq I in complex with the cofactor S-adenosylmethionine
    • Labahn, J., et al., & Saenger, W. (1994). Three-dimensional structure of the adenine-specific DNA methyltransferase M-Taq I in complex with the cofactor S-adenosylmethionine. Proc. Nat. Acad. Sci. USA 91, 10957-10961.
    • (1994) Proc. Nat. Acad. Sci. USA , vol.91 , pp. 10957-10961
    • Labahn, J.1    Saenger, W.2
  • 41
    • 0029068629 scopus 로고
    • The crystal structure of Haelll methyltransferase covalently complexed to DNA: An extrahelical cytosine and rearranged base pairing
    • Reinisch, K.M., Chen, L., Verdine, G.L. & Lipscomb, W.N. (1995). The crystal structure of Haelll methyltransferase covalently complexed to DNA: an extrahelical cytosine and rearranged base pairing. Cell 82, 143-153.
    • (1995) Cell , vol.82 , pp. 143-153
    • Reinisch, K.M.1    Chen, L.2    Verdine, G.L.3    Lipscomb, W.N.4
  • 42
    • 0029665054 scopus 로고    scopus 로고
    • The 1.85 Å structure of vaccinia protein VP39: A bifunctional enzyme that participates in the modification of both mRNA ends
    • Hodel, A.E., Gershon, P.D., Shi, X. & Quiocho, FA. (1996). The 1.85 Å structure of vaccinia protein VP39: a bifunctional enzyme that participates in the modification of both mRNA ends. Cell 85, 247-256.
    • (1996) Cell , vol.85 , pp. 247-256
    • Hodel, A.E.1    Gershon, P.D.2    Shi, X.3    Quiocho, F.A.4
  • 43
    • 0028210328 scopus 로고
    • Crystal structure of catechol O-methyltransferase
    • Vidgren, J., Svensson, L.A. & Liljas, A. (1994). Crystal structure of catechol O-methyltransferase. Nature 368, 354-358.
    • (1994) Nature , vol.368 , pp. 354-358
    • Vidgren, J.1    Svensson, L.A.2    Liljas, A.3
  • 44
    • 0015834475 scopus 로고
    • Comparison of super-secondary structure in proteins
    • Rao, S.T. & Rossmann, M.G. (1973). Comparison of super-secondary structure in proteins. J. Mol. Biol. 76, 241-256.
    • (1973) J. Mol. Biol. , vol.76 , pp. 241-256
    • Rao, S.T.1    Rossmann, M.G.2
  • 45
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding βαβ fold in proteins, using an amino acid sequence fingerprint
    • Wierenga, R.K., Terpstra, P. & Hol, W.G.J. (1986). Prediction of the occurrence of the ADP-binding βαβ fold in proteins, using an amino acid sequence fingerprint. J. Mol. Biol. 187, 101-107.
    • (1986) J. Mol. Biol. , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Terpstra, P.2    Hol, W.G.J.3
  • 46
    • 0024462909 scopus 로고
    • Three-dimensional crystal structures of Escherichia coli met repressor with and without corepressor
    • Rafferty, J.B., Somers, W.S., Saint-Girons, I. & Phillips. S.E.V. (1989). Three-dimensional crystal structures of Escherichia coli met repressor with and without corepressor. Nature 341, 705-710.
    • (1989) Nature , vol.341 , pp. 705-710
    • Rafferty, J.B.1    Somers, W.S.2    Saint-Girons, I.3    Phillips, S.E.V.4
  • 47
    • 0029876208 scopus 로고    scopus 로고
    • Structure and function of S-adenosylmethionine synthetase: Crystal structures of S-adenosylmethionine synthetase with ADP, BrADP, and PPi at 2.8 Å resolution
    • Takusagawa, F., Kamitori, S. & Markham, G.D. (1996). Structure and function of S-adenosylmethionine synthetase: crystal structures of S-adenosylmethionine synthetase with ADP, BrADP, and PPi at 2.8 Å resolution. Biochemistry 35, 2586-2596.
    • (1996) Biochemistry , vol.35 , pp. 2586-2596
    • Takusagawa, F.1    Kamitori, S.2    Markham, G.D.3
  • 49
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. & Sander, C. (1993). Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 50
    • 0020064853 scopus 로고
    • Routes of flavodoxin and ferredoxin reduction in Escherichia coli. CoA-acylating pyruvate:flavodoxin and NADPH :flavodoxin oxidoreductases participating in the activation of pyruvate formatelyase
    • Blaschkowski, H.P., Neuer, G., Ludwig-Festl, M. & Knappe, J. (1982). Routes of flavodoxin and ferredoxin reduction in Escherichia coli. CoA-acylating pyruvate:flavodoxin and NADPH :flavodoxin oxidoreductases participating in the activation of pyruvate formatelyase. Eur. J. Biochem. 123, 563-569.
    • (1982) Eur. J. Biochem. , vol.123 , pp. 563-569
    • Blaschkowski, H.P.1    Neuer, G.2    Ludwig-Festl, M.3    Knappe, J.4
  • 51
    • 0021296422 scopus 로고
    • Pyruvate formate-lyase (inactive form) and pyruvate formate-lyase activating enzyme of Escherichia coli: Isolation and structural properties
    • Conradt, H., Hohmann-Berger, M., Hohmann, H.P., Blaschkowski, H.P. & Knappe, J. (1984). Pyruvate formate-lyase (inactive form) and pyruvate formate-lyase activating enzyme of Escherichia coli: isolation and structural properties. Arch. Biochem. Biophys. 228, 133-142.
    • (1984) Arch. Biochem. Biophys. , vol.228 , pp. 133-142
    • Conradt, H.1    Hohmann-Berger, M.2    Hohmann, H.P.3    Blaschkowski, H.P.4    Knappe, J.5
  • 52
    • 0028275314 scopus 로고
    • Adenosylmethionine-dependent synthesis of the glycyl radical in pyruvate formate-lyase by abstraction of the glycine C-2 pro-S hydrogen atom
    • Frey, M., Rothe, M., Wagner, A.F.V. & Knappe, J. (1994). Adenosylmethionine-dependent synthesis of the glycyl radical in pyruvate formate-lyase by abstraction of the glycine C-2 pro-S hydrogen atom. J. Biol. Chem. 269, 12432-12437.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12432-12437
    • Frey, M.1    Rothe, M.2    Wagner, A.F.V.3    Knappe, J.4
  • 53
    • 0027771036 scopus 로고
    • Flavodoxin is required for the activation of the anaerobic ribonucleotide reductase
    • Bianchi, V., et al., & Reichard, P. (1993) Flavodoxin is required for the activation of the anaerobic ribonucleotide reductase. Biochem. Biophys. Res. Commun. 197, 792-797.
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 792-797
    • Bianchi, V.1    Reichard, P.2
  • 54
    • 0025363362 scopus 로고
    • The anaerobic ribonucleoside triphosphate reductase from Escherichia coli requires S-adenosylmethionine as a cofactor
    • Eliasson, R., Fontecave, M., Jörnvall, H., Krook, M., Pontis, & Reichard, P. (1990). The anaerobic ribonucleoside triphosphate reductase from Escherichia coli requires S-adenosylmethionine as a cofactor. Proc. Natl. Acad. Sci. USA 87, 3314-3318.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3314-3318
    • Eliasson, R.1    Fontecave, M.2    Jörnvall, H.3    Krook, M.4    Pontis5    Reichard, P.6
  • 55
    • 0027407871 scopus 로고
    • An ironsulfur center and a free radical in the active anaerobic ribonucleotide reductase of Escherichia coli
    • Mulliez, E., Fontcave, M., Gaillard, J. & Reichard, P. (1993). An ironsulfur center and a free radical in the active anaerobic ribonucleotide reductase of Escherichia coli. J. Biol. Chem. 268, 2296-2299.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2296-2299
    • Mulliez, E.1    Fontcave, M.2    Gaillard, J.3    Reichard, P.4
  • 56
    • 0028280411 scopus 로고
    • Biotin synthase: Purification, characterization as a [2Fe-2S] cluster protein, and in vitro activity of the Escherichia coli bioB gene product
    • Sanyal, I., Cohen, G. & Flint, D.H. (1994). Biotin synthase: purification, characterization as a [2Fe-2S] cluster protein, and in vitro activity of the Escherichia coli bioB gene product. Biochemistry 33, 3625-3631.
    • (1994) Biochemistry , vol.33 , pp. 3625-3631
    • Sanyal, I.1    Cohen, G.2    Flint, D.H.3
  • 57
    • 0028837286 scopus 로고
    • Generation of the glycyl radical of the anaerobic Escherichia coli ribonucleotide reductase requires a specific activation enzyme
    • Sun, X., et al., & Reichard, P. (1995). Generation of the glycyl radical of the anaerobic Escherichia coli ribonucleotide reductase requires a specific activation enzyme. J. Biol. Chem. 270, 2443-2446.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2443-2446
    • Sun, X.1    Reichard, P.2
  • 59
    • 0027729952 scopus 로고
    • Molecular properties of pyruvate formate-lyase activating enzyme
    • Wong, K.K., et al., & Kozarich, J. (1993). Molecular properties of pyruvate formate-lyase activating enzyme. Biochemistry 32, 14102-14110.
    • (1993) Biochemistry , vol.32 , pp. 14102-14110
    • Wong, K.K.1    Kozarich, J.2
  • 60
    • 0028104402 scopus 로고
    • Bacteriophage T4 gene 55.9 encodes an activity required for anaerobic ribonucleotide reduction
    • Young, P., Ohman, M. & Sjoberg, B.-M. (1994). Bacteriophage T4 gene 55.9 encodes an activity required for anaerobic ribonucleotide reduction. J. Biol. Chem. 269, 27815-27818.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27815-27818
    • Young, P.1    Ohman, M.2    Sjoberg, B.-M.3
  • 61
    • 0026690571 scopus 로고
    • A new approach to protein fold recognition
    • Jones, D.T., Taylor, W.R. & Thornton, J.M. (1992). A new approach to protein fold recognition. Nature 358, 86-89.
    • (1992) Nature , vol.358 , pp. 86-89
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 63
    • 0029670933 scopus 로고    scopus 로고
    • 12-binding region of methionine synthase: How the protein controls methylcobalamin reactivity
    • 12-binding region of methionine synthase: how the protein controls methylcobalamin reactivity. Biochemistry 35, 2464-2475.
    • (1996) Biochemistry , vol.35 , pp. 2464-2475
    • Jarrett, J.T.1    Matthews, R.G.2
  • 65
    • 0000443712 scopus 로고
    • Inherited disorders of folate transport and metabolism
    • Scriver, C.R., Beaudet, A.L., Sly, W.S. & Valle, D., eds. McGraw-Hill, New York
    • Rosenblatt, D.S. (1995). Inherited disorders of folate transport and metabolism. In Metabolic Bases of Inherited Disease, Vol. II (Scriver, C.R., Beaudet, A.L., Sly, W.S. & Valle, D., eds.), pp. 3111 -3128, McGraw-Hill, New York.
    • (1995) Metabolic Bases of Inherited Disease , vol.2 , pp. 3111-3128
    • Rosenblatt, D.S.1
  • 66
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B.W. (1968). Solvent content of protein crystals. J. Mol. Biol. 33, 491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 67
    • 0000134034 scopus 로고
    • Strategyfor data collection from protein crystals using a multiwire counter area detector diffractometer
    • Howard, A.J., Nielson, C. & Xuong, N.H. (1985). Strategyfor data collection from protein crystals using a multiwire counter area detector diffractometer. J. Appl. Cryst. 18, 342-350.
    • (1985) J. Appl. Cryst. , vol.18 , pp. 342-350
    • Howard, A.J.1    Nielson, C.2    Xuong, N.H.3
  • 68
    • 0001473634 scopus 로고
    • Unbiased three-dimensional refinement of heavy-atom parameters by correlation of origin-removed patterson functions
    • Terwilliger, T.C. & Eisenberg, D. (1983) Unbiased three-dimensional refinement of heavy-atom parameters by correlation of origin-removed patterson functions. Acta Cryst. A 39, 813-817.
    • (1983) Acta Cryst. A , vol.39 , pp. 813-817
    • Terwilliger, T.C.1    Eisenberg, D.2
  • 69
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy atom parameters
    • Wolf, W., Evans, P.R.E. & Leslie, A.G., eds SERC Daresbury Laboratory, Warrington, UK
    • Otwinowsky, Z. (1991 ). Maximum likelihood refinement of heavy atom parameters. In Isomorphous Replacement and Anomalous Scattering. (Wolf, W., Evans, P.R.E. & Leslie, A.G., eds), pp. 80-86, SERC Daresbury Laboratory, Warrington, UK.
    • (1991) Isomorphous Replacement and Anomalous Scattering , pp. 80-86
    • Otwinowsky, Z.1
  • 70
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computation Project, Number 4
    • Collaborative Computation Project, Number 4. (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 72
    • 45949114594 scopus 로고
    • TOM: A FRODO subpackage for protein-ligand fitting with interactive energy minimization
    • Cambillau, C. & Horjales, E. (1987). TOM: a FRODO subpackage for protein-ligand fitting with interactive energy minimization. J. Mol. Graph. 5, 174-177.
    • (1987) J. Mol. Graph. , vol.5 , pp. 174-177
    • Cambillau, C.1    Horjales, E.2
  • 73
    • 0001797984 scopus 로고
    • FRODO: A graphics fitting program for macromolecules
    • Sayre, D., ed Clarendon Press, Oxford, UK
    • Jones, TA (1982). FRODO: a graphics fitting program for macromolecules. In Crystallographic Computing. (Sayre, D., ed), pp. 303-317, Clarendon Press, Oxford, UK.
    • (1982) Crystallographic Computing , pp. 303-317
    • Jones, T.A.1
  • 75
    • 84944812409 scopus 로고
    • Improved fourier coefficients for maps using phases from partial structures with errors
    • Read, R. (1986). Improved fourier coefficients for maps using phases from partial structures with errors. Acta Cryst. A 42, 140-149.
    • (1986) Acta Cryst. A , vol.42 , pp. 140-149
    • Read, R.1
  • 76
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 77
    • 0000913086 scopus 로고
    • A fast algorithm for rendering space-filling molecule pictures
    • Bacon, B. & Anderson, W.F. (1988). A fast algorithm for rendering space-filling molecule pictures. J. Mol. Graphics 6, 219-220.
    • (1988) J. Mol. Graphics , vol.6 , pp. 219-220
    • Bacon, B.1    Anderson, W.F.2
  • 78
    • 0028057108 scopus 로고
    • Raster3D Version 2.0: A program for photorealistic molecular graphics
    • Merritt, E.A. & Murphy, M.E.P. (1994). Raster3D Version 2.0: a program for photorealistic molecular graphics. Acta Cryst. D 50, 869-873.
    • (1994) Acta Cryst. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 79
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. & Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 80
    • 0025271319 scopus 로고
    • Nucleotide sequence of the metH gene of Escherichia coli K-12 and comparison with that of Salmonella typhimurium LT2
    • Old, I.G., Margarita, D., Glass, R.E. & Saint Girons I. (1990). Nucleotide sequence of the metH gene of Escherichia coli K-12 and comparison with that of Salmonella typhimurium LT2. Gene 87, 15-21.
    • (1990) Gene , vol.87 , pp. 15-21
    • Old, I.G.1    Margarita, D.2    Glass, R.E.3    Saint Girons, I.4
  • 81
    • 0027485897 scopus 로고
    • Electrospray mass spectrometric analysis of the domains of a large enzyme: Observation of the occupied cobalamin-binding domain and redefinition of the carboxyl terminus of methionine synthase
    • Drummond, J.T., Orgorzalek Loo, R.R. & Matthews, R.G. (1993). Electrospray mass spectrometric analysis of the domains of a large enzyme: observation of the occupied cobalamin-binding domain and redefinition of the carboxyl terminus of methionine synthase. Biochemistry 32, 9282-9289.
    • (1993) Biochemistry , vol.32 , pp. 9282-9289
    • Drummond, J.T.1    Orgorzalek Loo, R.R.2    Matthews, R.G.3
  • 82
    • 0029653518 scopus 로고
    • Whole-genome random sequencing and assembly of Haemophilus influenzae Rd
    • Fleischmann, R.D., et al., & Venter, J.C. (1995). Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science 269, 496-512.
    • (1995) Science , vol.269 , pp. 496-512
    • Fleischmann, R.D.1    Venter, J.C.2
  • 83
    • 0029655167 scopus 로고
    • Sequence analysis of the genome of the unicellular cyanbacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome
    • Kaneko, T., et al., & Tabata, S. (1995). Sequence analysis of the genome of the unicellular cyanbacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome. DNA Res. 2, 153-166.
    • (1995) DNA Res. , vol.2 , pp. 153-166
    • Kaneko, T.1    Tabata, S.2
  • 84
    • 0026030641 scopus 로고
    • Database of homology-derived protein structures and the structural meaning of sequence alignment
    • Sander, C. & Schneider, R. (1991). Database of homology-derived protein structures and the structural meaning of sequence alignment. Proteins 9, 56-68.
    • (1991) Proteins , vol.9 , pp. 56-68
    • Sander, C.1    Schneider, R.2
  • 85
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4


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