메뉴 건너뛰기




Volumn 47, Issue 36, 2008, Pages 9608-9617

Structural basis for substrate specificity in phosphate binding (β/α)8-barrels: D-allulose 6-phosphate 3-epimerase from Escherichia coli K-12

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHATE BINDING; STRUCTURAL BASIS; SUBSTRATE SPECIFICITY;

EID: 51549112289     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800821v     Document Type: Article
Times cited : (16)

References (27)
  • 1
    • 0036384350 scopus 로고    scopus 로고
    • One fold with many functions: The evolutionary relationships between TIM barrel families based on their sequences, structures and functions
    • Nagano, N., Orengo, C. A., and Thornton, J. M. (2002) One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions. J. Mol. Biol. 321, 741-765.
    • (2002) J. Mol. Biol , vol.321 , pp. 741-765
    • Nagano, N.1    Orengo, C.A.2    Thornton, J.M.3
  • 3
    • 0034284955 scopus 로고    scopus 로고
    • Structural evidence for evolution of the β/α barrel scaffold by gene duplication and fusion
    • Lang, D., Thoma, R., Henn-Sax, M., Sterner, R., and Wilmanns, M. (2000) Structural evidence for evolution of the β/α barrel scaffold by gene duplication and fusion. Science 289, 1546-1550.
    • (2000) Science , vol.289 , pp. 1546-1550
    • Lang, D.1    Thoma, R.2    Henn-Sax, M.3    Sterner, R.4    Wilmanns, M.5
  • 5
    • 0028955737 scopus 로고
    • Divergent evolution of a beta/alpha-barrel subclass: Detection of numerous phosphate-binding sites by motif search
    • Bork, P., Gellerich, J., Groth, H., Hooft, R., and Martin, F. (1995) Divergent evolution of a beta/alpha-barrel subclass: detection of numerous phosphate-binding sites by motif search. Protein Sci. 4, 268-274.
    • (1995) Protein Sci , vol.4 , pp. 268-274
    • Bork, P.1    Gellerich, J.2    Groth, H.3    Hooft, R.4    Martin, F.5
  • 6
    • 0037116603 scopus 로고    scopus 로고
    • A common evolutionary origin of two elementary enzyme folds
    • Hocker, B., Schmidt, S., and Sterner, R. (2002) A common evolutionary origin of two elementary enzyme folds. FEBS Lett. 510, 133-135.
    • (2002) FEBS Lett , vol.510 , pp. 133-135
    • Hocker, B.1    Schmidt, S.2    Sterner, R.3
  • 8
    • 0034053002 scopus 로고    scopus 로고
    • New wine from old barrels [news]
    • Gerlt, J. A. (2000) New wine from old barrels [news]. Nat. Struct. Biol. 7, 171-173.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 171-173
    • Gerlt, J.A.1
  • 9
    • 3242882336 scopus 로고    scopus 로고
    • AdoMet radical proteins-from structure to evolution-alignment of divergent protein sequences reveals strong secondary structure element conservation
    • Nicolet, Y., and Drennan, C. L. (2004) AdoMet radical proteins-from structure to evolution-alignment of divergent protein sequences reveals strong secondary structure element conservation. Nucleic Acids Res. 32, 4015-4025.
    • (2004) Nucleic Acids Res , vol.32 , pp. 4015-4025
    • Nicolet, Y.1    Drennan, C.L.2
  • 10
    • 33644499463 scopus 로고    scopus 로고
    • D-Ribulose 5-phosphate 3-epimerase: Functional and structural relationships to members of the ribulose-phosphate binding (beta/alpha)8-barrel superfamily
    • Akana, J., Fedorov, A. A., Fedorov, E., Novak, W. R., Babbitt, P. C., Almo, S. C., and Gerlt, J. A. (2006) D-Ribulose 5-phosphate 3-epimerase: functional and structural relationships to members of the ribulose-phosphate binding (beta/alpha)8-barrel superfamily. Biochemistry 45, 2493-2503.
    • (2006) Biochemistry , vol.45 , pp. 2493-2503
    • Akana, J.1    Fedorov, A.A.2    Fedorov, E.3    Novak, W.R.4    Babbitt, P.C.5    Almo, S.C.6    Gerlt, J.A.7
  • 11
    • 0035861072 scopus 로고    scopus 로고
    • Contribution of phosphate intrinsic binding energy to the enzymatic rate acceleration for triosephosphate isomerase
    • Amyes, T. L., O'Donoghue, A. C., and Richard, J. P. (2001) Contribution of phosphate intrinsic binding energy to the enzymatic rate acceleration for triosephosphate isomerase. J. Am. Chem. Soc. 123, 11325-11326.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 11325-11326
    • Amyes, T.L.1    O'Donoghue, A.C.2    Richard, J.P.3
  • 12
    • 27844574242 scopus 로고    scopus 로고
    • Activation of orotidine 5′-monophosphate decarboxylase by phosphite dianion: The whole substrate is the sum of two parts
    • Amyes, T. L., Richard, J. P., and Tait, J. J. (2005) Activation of orotidine 5′-monophosphate decarboxylase by phosphite dianion: the whole substrate is the sum of two parts. J. Am. Chem. Soc. 127, 15708-15709.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 15708-15709
    • Amyes, T.L.1    Richard, J.P.2    Tait, J.J.3
  • 13
    • 0025882959 scopus 로고
    • Structure of the triosephosphate isomerase- phosphoglycolohydroxamate complex: An analogue of the intermediate on the reaction pathway
    • Davenport, R. C., Bash, P. A., Seaton, B. A., Karplus, M., Petsko, G. A., and Ringe, D. (1991) Structure of the triosephosphate isomerase- phosphoglycolohydroxamate complex: an analogue of the intermediate on the reaction pathway. Biochemistry 30, 5821-5826.
    • (1991) Biochemistry , vol.30 , pp. 5821-5826
    • Davenport, R.C.1    Bash, P.A.2    Seaton, B.A.3    Karplus, M.4    Petsko, G.A.5    Ringe, D.6
  • 14
    • 0034058368 scopus 로고    scopus 로고
    • The crystal structure and mechanism of orotidine 5′-monophosphate decarboxylase
    • Appleby, T. C., Kinsland, C., Begley, T. P., and Ealick, S. E. (2000) The crystal structure and mechanism of orotidine 5′-monophosphate decarboxylase. Proc. Natl. Acad. Sci. U.S.A. 97 2005-2010.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 2005-2010
    • Appleby, T.C.1    Kinsland, C.2    Begley, T.P.3    Ealick, S.E.4
  • 15
    • 43649086695 scopus 로고    scopus 로고
    • Phosphate Binding Energy and Catalysis by Small and Large Molecules
    • Morrow, J. R., Amyes, T. L., and Richard, J. P. (2008) Phosphate Binding Energy and Catalysis by Small and Large Molecules. Acc. Chem. Res. 41, 539-548.
    • (2008) Acc. Chem. Res , vol.41 , pp. 539-548
    • Morrow, J.R.1    Amyes, T.L.2    Richard, J.P.3
  • 16
    • 0030735584 scopus 로고    scopus 로고
    • The D-allose operon of Escherichia coli K-12
    • Kim, C., Song, S., and Park, C. (1997) The D-allose operon of Escherichia coli K-12. J. Bacteriol. 179, 7631-7637.
    • (1997) J. Bacteriol , vol.179 , pp. 7631-7637
    • Kim, C.1    Song, S.2    Park, C.3
  • 17
    • 36749023905 scopus 로고    scopus 로고
    • Divergent evolution of function in the ROK sugar kinase superfamily: Role of enzyme loops in substrate specificity
    • Larion, M., Moore, L. B., Thompson, S. M., and Miller, B. G. (2007) Divergent evolution of function in the ROK sugar kinase superfamily: role of enzyme loops in substrate specificity. Biochemistry 46, 13564-13572.
    • (2007) Biochemistry , vol.46 , pp. 13564-13572
    • Larion, M.1    Moore, L.B.2    Thompson, S.M.3    Miller, B.G.4
  • 18
    • 23844503225 scopus 로고    scopus 로고
    • Reconstitution of a defunct glycolytic pathway via recruitment of ambiguous sugar kinases
    • Miller, B. G., and Raines, R. T. (2005) Reconstitution of a defunct glycolytic pathway via recruitment of ambiguous sugar kinases. Biochemistry 44, 10776-10783.
    • (2005) Biochemistry , vol.44 , pp. 10776-10783
    • Miller, B.G.1    Raines, R.T.2
  • 19
    • 0343879238 scopus 로고
    • Assay of Inorganic Phosphate, Total Phosphate and Phosphatases
    • Ames, B. N. (1966) Assay of Inorganic Phosphate, Total Phosphate and Phosphatases. Methods Enzymol 8, 115-118.
    • (1966) Methods Enzymol , vol.8 , pp. 115-118
    • Ames, B.N.1
  • 20
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and Wanner, B. L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U.S.A. 97, 6640-6645.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 21
    • 0035951059 scopus 로고    scopus 로고
    • Evolution of Enzymatic Activities in the Enolase Superfamily: Functional Assignment of Unknown Proteins in Bacillus subtilis and Escherichia coli as L-Ala-D/L-Glu Epimerases
    • Schmidt, D. M., Hubbard, B. K., and Gerlt, J. A. (2001) Evolution of Enzymatic Activities in the Enolase Superfamily: Functional Assignment of Unknown Proteins in Bacillus subtilis and Escherichia coli as L-Ala-D/L-Glu Epimerases. Biochemistry 40, 15707-15715.
    • (2001) Biochemistry , vol.40 , pp. 15707-15715
    • Schmidt, D.M.1    Hubbard, B.K.2    Gerlt, J.A.3
  • 22
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Carter, C. W. J, Sweet, R. M, Abelson, J. N, and Simon, M. I, Eds, pp, Academic Pres, New York
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, in Methods in Enzymology (Carter, C. W. J., Sweet, R. M., Abelson, J. N., and Simon, M. I., Eds.) pp 307-326, Academic Pres, New York.
    • (1997) Methods in Enzymology , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 25
    • 0022333120 scopus 로고
    • Interactive computer graphics: FRODO
    • Jones, A. T. (1985) Interactive computer graphics: FRODO. Methods Enzymol. 115, 157-171.
    • (1985) Methods Enzymol , vol.115 , pp. 157-171
    • Jones, A.T.1
  • 26
    • 0037134514 scopus 로고    scopus 로고
    • Hinge-bending motion of D-allose-binding protein from Escherichia coli: Three open conformations
    • Magnusson, U., Chaudhuri, B. N., Ko, J., Park, C., Jones, T. A., and Mowbray, S. L. (2002) Hinge-bending motion of D-allose-binding protein from Escherichia coli: three open conformations. J. Biol. Chem. 277, 14077-84.
    • (2002) J. Biol. Chem , vol.277 , pp. 14077-14084
    • Magnusson, U.1    Chaudhuri, B.N.2    Ko, J.3    Park, C.4    Jones, T.A.5    Mowbray, S.L.6
  • 27
    • 0033548701 scopus 로고    scopus 로고
    • Structure of D-allose binding protein from Escherichia coli bound to D-allose at 1.8 A resolution
    • Chaudhuri, B. N., Ko, J., Park, C., Jones, T. A., and Mowbray, S. L. (1999) Structure of D-allose binding protein from Escherichia coli bound to D-allose at 1.8 A resolution. J. Mol. Biol. 286, 1519-31.
    • (1999) J. Mol. Biol , vol.286 , pp. 1519-1531
    • Chaudhuri, B.N.1    Ko, J.2    Park, C.3    Jones, T.A.4    Mowbray, S.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.