메뉴 건너뛰기




Volumn 288, Issue 5, 1999, Pages 989-998

Crystal structure of the hydrogenase maturating endopeptidase HYBD from Escherichia coli

Author keywords

Hydrogenase; Maturation; Metzincins; Nickel; Protease

Indexed keywords

ASPARTIC ACID; GLUTAMIC ACID; HISTIDINE; HYDROGENASE; NICKEL; PROTEINASE;

EID: 0033591263     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2719     Document Type: Article
Times cited : (81)

References (45)
  • 1
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1-ATPase
    • Abrahams J. P., Leslie A. G. W. Methods used in the structure determination of bovine mitochondrial F1-ATPase. Acta Crystallog. sect. D. 52:1996;30-42.
    • (1996) Acta Crystallog. Sect. D , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.W.2
  • 2
    • 0030725104 scopus 로고    scopus 로고
    • A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system
    • Andrews S. C., Berks B. C., McClay J., Ambler A., Quail M. A., Golby P., Guest J. R. A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system. Microbiology. 143:1997;3633-3647.
    • (1997) Microbiology , vol.143 , pp. 3633-3647
    • Andrews, S.C.1    Berks, B.C.2    McClay, J.3    Ambler, A.4    Quail, M.A.5    Golby, P.6    Guest, J.R.7
  • 3
    • 85030352979 scopus 로고    scopus 로고
    • Barton. 1993
    • Barton. 1993.
  • 4
    • 0030045930 scopus 로고    scopus 로고
    • Nickel incorporation into hydrogenase 3 from Escherichia coli requires the precursor form of the large subunit
    • Binder U., Maier T., Böck A. Nickel incorporation into hydrogenase 3 from Escherichia coli requires the precursor form of the large subunit. Arch. Microbiol. 165:1996;69-72.
    • (1996) Arch. Microbiol. , vol.165 , pp. 69-72
    • Binder, U.1    Maier, T.2    Böck, A.3
  • 5
    • 0027515396 scopus 로고
    • Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the "metzincins"
    • Bode W., Gomis-Rüth F. X., Stöcker W. Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the "metzincins" FEBS Letters. 331:1993;134-140.
    • (1993) FEBS Letters , vol.331 , pp. 134-140
    • Bode, W.1    Gomis-Rüth, F.X.2    Stöcker, W.3
  • 6
    • 0025157053 scopus 로고
    • Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components
    • Böhm R., Sauter M., Böck A. Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components. Mol. Microbiol. 4:1990;231-243.
    • (1990) Mol. Microbiol. , vol.4 , pp. 231-243
    • Böhm, R.1    Sauter, M.2    Böck, A.3
  • 9
    • 0345647107 scopus 로고    scopus 로고
    • Interaction of the hydrogenase accessory protein HypC with HycE, the large subunit of Escherichia coli hydrogenase 3 during enzyme maturation
    • Drapal N., Böck A. Interaction of the hydrogenase accessory protein HypC with HycE, the large subunit of Escherichia coli hydrogenase 3 during enzyme maturation. Biochemistry. 37:1998;2941-2948.
    • (1998) Biochemistry , vol.37 , pp. 2941-2948
    • Drapal, N.1    Böck, A.2
  • 10
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh R. A., Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallog. sect. A. 47:1991;392-400.
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 11
    • 0030726657 scopus 로고    scopus 로고
    • Crystal structure of methyl-coenzyme M reductase: The key enzyme of biological methane formation
    • Ermler U., Grabarse W., Shima S., Goubeaud M., Thauer R. K. Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation. Science. 278:1997;1457-1462.
    • (1997) Science , vol.278 , pp. 1457-1462
    • Ermler, U.1    Grabarse, W.2    Shima, S.3    Goubeaud, M.4    Thauer, R.K.5
  • 12
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representations of macromolecules
    • Evans S. V. SETOR: Hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11:1993;134-138.
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 13
    • 0027382485 scopus 로고
    • Molecular biology of hydrogen utilization in aerobic chemolithotrophs
    • Friedrich B., Schwartz E. Molecular biology of hydrogen utilization in aerobic chemolithotrophs. Annu. Rev. Microbiol. 47:1993;351-383.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 351-383
    • Friedrich, B.1    Schwartz, E.2
  • 15
    • 0026714545 scopus 로고
    • Carboxyl-terminal processing may be essential for production of active NiFe hydrogenase in Azotobacter vinelandii
    • Gollin D. J., Mortenson L. E., Robson R. L. Carboxyl-terminal processing may be essential for production of active NiFe hydrogenase in Azotobacter vinelandii. FEBS Letters. 309:1992;371-375.
    • (1992) FEBS Letters , vol.309 , pp. 371-375
    • Gollin, D.J.1    Mortenson, L.E.2    Robson, R.L.3
  • 17
    • 0031574022 scopus 로고    scopus 로고
    • Unusual ligand structure in Ni-Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis
    • Higuchi Y., Yagi T., Yasuoka N. Unusual ligand structure in Ni-Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis. Structure. 5:1997;1671-1680.
    • (1997) Structure , vol.5 , pp. 1671-1680
    • Higuchi, Y.1    Yagi, T.2    Yasuoka, N.3
  • 18
    • 0029647957 scopus 로고
    • The crystal structure of urease from Klebsiella aerogenes
    • Jabri E., Carr M. B., Hausinger R. P., Karplus P. A. The crystal structure of urease from Klebsiella aerogenes. Science. 268:1995;998-1004.
    • (1995) Science , vol.268 , pp. 998-1004
    • Jabri, E.1    Carr, M.B.2    Hausinger, R.P.3    Karplus, P.A.4
  • 19
    • 0000356656 scopus 로고
    • A graphics model building and refinement system for macromolecules
    • Jones T. A. A graphics model building and refinement system for macromolecules. J. Appl. Crystallog. 11:1978;268-272.
    • (1978) J. Appl. Crystallog. , vol.11 , pp. 268-272
    • Jones, T.A.1
  • 20
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 21
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • R. M. Sweet, & C. W. Jr. Carter. New York: Academic Press
    • La Fortelle E., Bricogne G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Sweet R. M., Carter C. W. Jr. Methods Enzymology, Macromolecular Crystallography. 1997;Academic Press, New York.
    • (1997) Methods Enzymology, Macromolecular Crystallography
    • La Fortelle, E.1    Bricogne, G.2
  • 25
    • 0029757989 scopus 로고    scopus 로고
    • Generation of active [NiFe] hydrogenase in vitro from a nickel-free precursor form
    • Maier T., Böck A. Generation of active [NiFe] hydrogenase in vitro from a nickel-free precursor form. Biochemistry. 35:1996;10089-10093.
    • (1996) Biochemistry , vol.35 , pp. 10089-10093
    • Maier, T.1    Böck, A.2
  • 26
    • 0027450599 scopus 로고
    • The product of the hyp B gene, which is required for nickel incorporation into hydrogenases, is a novel guanine nucleotide-binding protein
    • Maier T., Jacobi A., Sauter M., Böck A. The product of the hyp B gene, which is required for nickel incorporation into hydrogenases, is a novel guanine nucleotide-binding protein. J. Bacteriol. 175:1993;630-635.
    • (1993) J. Bacteriol. , vol.175 , pp. 630-635
    • Maier, T.1    Jacobi, A.2    Sauter, M.3    Böck, A.4
  • 27
    • 0029054222 scopus 로고
    • GTP hydrolysis by HypB is essential for nickel insertion into hydrogenases of Escherichia coli
    • Maier T., Lottspeich F., Böck A. GTP hydrolysis by HypB is essential for nickel insertion into hydrogenases of Escherichia coli. Eur. J. Biochem. 230:1995;133-138.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 133-138
    • Maier, T.1    Lottspeich, F.2    Böck, A.3
  • 28
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B. W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 29
    • 0028157325 scopus 로고
    • In vivo and in vitro nickel-dependent processing of the [NiFe] hydrogenase inAzotobacter vinelandii
    • Menon A. L., Robson R. L. In vivo and in vitro nickel-dependent processing of the [NiFe] hydrogenase inAzotobacter vinelandii. J. Bacteriol. 176:1994;291-295.
    • (1994) J. Bacteriol. , vol.176 , pp. 291-295
    • Menon, A.L.1    Robson, R.L.2
  • 30
    • 0025366313 scopus 로고
    • Cloning and sequencing of a putative Escherichia coli[NiFe] hydrogenase-1 operon containing six open reading frames
    • Menon N. K., Robbins J., Peck H. D. Jr, Chatelus C. Y., Choi E. S., Przybyla A. E. Cloning and sequencing of a putative Escherichia coli[NiFe] hydrogenase-1 operon containing six open reading frames. J. Bacteriol. 172:1990;1969-1977.
    • (1990) J. Bacteriol. , vol.172 , pp. 1969-1977
    • Menon, N.K.1    Robbins, J.2    Peck H.D., Jr.3    Chatelus, C.Y.4    Choi, E.S.5    Przybyla, A.E.6
  • 33
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G. N., Vagin A. A., Dodson E. J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystalog. sect D. 53:1997;240-255.
    • (1997) Acta Crystalog. Sect D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 35
    • 0026814596 scopus 로고
    • Structure-function relationships among the nickel-containing hydrogenases
    • Przybyla A. E., Robbins J., Menon N., Peck H. D. Jr. Structure-function relationships among the nickel-containing hydrogenases. FEMS Microbiol. Rev. 88:1992;109-136.
    • (1992) FEMS Microbiol. Rev. , vol.88 , pp. 109-136
    • Przybyla, A.E.1    Robbins, J.2    Menon, N.3    Peck H.D., Jr.4
  • 36
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson J. S. The anatomy and taxonomy of protein structure. Advan. Protein Chem. 34:1981;167-339.
    • (1981) Advan. Protein Chem. , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 37
    • 0028314544 scopus 로고
    • Maturation of the large subunit (HYCE) of Escherichia coli hydrogenase 3 requires nickel incorporation followed by C-terminal processing at Arg537
    • Rossmann R., Sauter M., Lottspeich F., Böck A. Maturation of the large subunit (HYCE) of Escherichia coli hydrogenase 3 requires nickel incorporation followed by C-terminal processing at Arg537. Eur. J. Biochem. 220:1994;377-384.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 377-384
    • Rossmann, R.1    Sauter, M.2    Lottspeich, F.3    Böck, A.4
  • 38
    • 0028832110 scopus 로고
    • Characterisation of a protease from Escherichia coli involved in hydrogenase maturation
    • Rossmann R., Maier T., Lottspeich F., Böck A. Characterisation of a protease from Escherichia coli involved in hydrogenase maturation. Eur. J. Biochem. 227:1995;545-550.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 545-550
    • Rossmann, R.1    Maier, T.2    Lottspeich, F.3    Böck, A.4
  • 39
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:1987;368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 40
    • 0000728003 scopus 로고
    • Tutorial on automated Patterson interpretation to find heavy atoms
    • D. Moras, A. D. Podjarny, & J. C. Thierry. Oxford: Oxford University Press
    • Sheldrick G. Tutorial on automated Patterson interpretation to find heavy atoms. Moras D., Podjarny A. D., Thierry J. C. Crystallographic Computing 5. 1991;145-157 Oxford University Press, Oxford.
    • (1991) Crystallographic Computing 5 , pp. 145-157
    • Sheldrick, G.1
  • 41
    • 0027233609 scopus 로고
    • A novel very small subunit of a selenium containing [NiFe] hydrogenase of Methanococcus voltae is posttranslationally processed by cleavage at a defined position
    • Sorgenfrei O., Linder D., Karas M., Klein A. A novel very small subunit of a selenium containing [NiFe] hydrogenase of Methanococcus voltae is posttranslationally processed by cleavage at a defined position. Eur. J. Biochem. 213:1993;1355-1358.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 1355-1358
    • Sorgenfrei, O.1    Linder, D.2    Karas, M.3    Klein, A.4
  • 42
    • 0028969678 scopus 로고
    • The metzincins - topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases
    • Stöcker W., Grams F., Baumann U., Reinemer P., Gomis-Rüth F. X., McKay D. B., Bode W. The metzincins - topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. Protein Sci. 4:1995;823-840.
    • (1995) Protein Sci. , vol.4 , pp. 823-840
    • Stöcker, W.1    Grams, F.2    Baumann, U.3    Reinemer, P.4    Gomis-Rüth, F.X.5    McKay, D.B.6    Bode, W.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.