메뉴 건너뛰기




Volumn 149, Issue 6, 2011, Pages 701-712

Crystal structure of serine dehydrogenase from Escherichia coli: Important role of the C-terminal region for closed-complex formation

Author keywords

conformational change; crystal structure; serine dehydrogenase; short chain dehydrogenase reductase family; substrate recognition

Indexed keywords

GLYCINE; HOMOSERINE DEHYDROGENASE; LEUCINE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; THREONINE; VALINE;

EID: 79957820871     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvr024     Document Type: Article
Times cited : (19)

References (25)
  • 1
    • 0037474227 scopus 로고    scopus 로고
    • Characterization of short-chain dehydrogenase/reductase homologues of Escherichia coli (YdfG) and Saccharomyces cerevisiae (YMR226C)
    • DOI 10.1016/S1570-9639(02)00533-2, PII S1570963902005332
    • Fujisawa, H., Nagata, S., and Misono, H. (2003) Characterization of short-chain dehydrogenase/reductase homologues of Escherichia coli (YdfG) and Saccharomyces cerevisiae (YMR226C). Biochim. Biophys. Acta 1645, 89-94 (Pubitemid 38234719)
    • (2003) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1645 , Issue.1 , pp. 89-94
    • Fujisawa, H.1    Nagata, S.2    Misono, H.3
  • 2
    • 77955969370 scopus 로고    scopus 로고
    • The Rut pathway for pyrimidine degradation: Novel chemistry and toxicity problems
    • Kim, K-S., Pelton, J.G., Inwood, W.B., Andersen, U., Kutsyu, S., and Wemmer, D.E. (2010) The Rut pathway for pyrimidine degradation: novel chemistry and toxicity problems. J. Bacteriol. 192, 4089-4102
    • (2010) J. Bacteriol. , vol.192 , pp. 4089-4102
    • Kim, K.-S.1    Pelton, J.G.2    Inwood, W.B.3    Andersen, U.4    Kutsyu, S.5    Wemmer, D.E.6
  • 4
    • 0035022533 scopus 로고    scopus 로고
    • SDR: Structure, mechanism of action, and substrate recognition
    • DOI 10.2174/1385272013375751
    • Tanaka, N., Nonaka, T., Nakamura, K.T., and Hara, A. (2001) SDR: structure, mechanism of action, and substrate recognition. Curr. Org. Chem. 5, 89-111 (Pubitemid 32421676)
    • (2001) Current Organic Chemistry , vol.5 , Issue.1 , pp. 89-111
    • Tanaka, N.1
  • 5
    • 0037324955 scopus 로고    scopus 로고
    • Coenzyme-based functional assignments of short-chain dehydrogenases/ reductases (SDRs)
    • DOI 10.1016/S0009-2797(02)00223-5, PII S0009279702002235
    • Persson, B., Kallberg, Y., Oppermann, U., and Jörnvall, H. (2003) Coenzyme-based functional assignments of short-chain dehydrogenase/reductases (SDRs). Chem. Biol. Interact. 143-144, 271-278 (Pubitemid 36253590)
    • (2003) Chemico-Biological Interactions , vol.143-144 , pp. 271-278
    • Persson, B.1    Kallberg, Y.2    Oppermann, U.3    Jornvall, H.4
  • 7
    • 29144458896 scopus 로고    scopus 로고
    • D-3-hydroxybutyrate dehydrogenase from Pseudomonas fragi: Molecular cloning of the enzyme gene and crystal structure of the enzyme
    • DOI 10.1016/j.jmb.2005.10.072, PII S002228360501332X
    • Ito, K., Nakajima, Y., Ichihara, E., Ogawa, K., Katayama, N., Nakashima, K., and Yoshimoto, T. (2006) D-3-Hydroxybutyrate Dehydrogenase from Pseudomonas fragi: Molecular cloning of the enzyme gene and crystal structure of the enzyme. J. Mol. Biol. 355, 722-733 (Pubitemid 41817632)
    • (2006) Journal of Molecular Biology , vol.355 , Issue.4 , pp. 722-733
    • Ito, K.1    Nakajima, Y.2    Ichihara, E.3    Ogawa, K.4    Katayama, N.5    Nakashima, K.6    Yoshimoto, T.7
  • 8
    • 0030000879 scopus 로고    scopus 로고
    • Crystal structures of the binary and ternary complexes of 7α-hydroxysteroid dehydrogenase from Escherichia coli
    • Tanaka, N., Nonaka, T., Tanabe, T., Yoshimoto, T., Tsuru, D., and Mitsui, Y. (1996) Crystal structures of the binary and ternary complexes of 7α-hydroxysteroid dehydrogenase from Escherichia coli. Biochemistry 35, 7715-7730
    • (1996) Biochemistry , vol.35 , pp. 7715-7730
    • Tanaka, N.1    Nonaka, T.2    Tanabe, T.3    Yoshimoto, T.4    Tsuru, D.5    Mitsui, Y.6
  • 9
    • 67649658200 scopus 로고    scopus 로고
    • Closed complex of the D-3-Hydroxybutyrate dehydrogenase induced by an enantiomeric competitive inhibitor
    • Nakashima, K., Ito, K., Nakajima, Y., Yamazawa, R., Miyakawa, S., and Yoshimoto, T. (2009) Closed complex of the D-3-Hydroxybutyrate dehydrogenase induced by an enantiomeric competitive inhibitor. J. Biochem. 145, 467-479
    • (2009) J. Biochem. , vol.145 , pp. 467-479
    • Nakashima, K.1    Ito, K.2    Nakajima, Y.3    Yamazawa, R.4    Miyakawa, S.5    Yoshimoto, T.6
  • 11
    • 0030040590 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic studies of 7α-hydroxysteroid dehydrogenase from Escherichia coli
    • Tanaka, N., Nonaka, T., Yoshimoto, T., Tsuru, D., and Mitsui, Y. (1996) Crystallization and preliminary X-ray crystallographic studies of 7α-hydroxysteroid dehydrogenase from Escherichia coli. Acta Crystallogr. Sect, D Biol. Crystallogr 52, 215-217
    • (1996) Acta Crystallogr. Sect, D Biol. Crystallogr , vol.52 , pp. 215-217
    • Tanaka, N.1    Nonaka, T.2    Yoshimoto, T.3    Tsuru, D.4    Mitsui, Y.5
  • 13
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 14
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4.
    • Collaborative Computational Project, Number 4. (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D Biol. Crystallogr. 50, 760-763
    • (1994) Acta Crystallogr. Sect. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 17
    • 0030743251 scopus 로고    scopus 로고
    • Rapid and efficient site-directed mutagenesis by single-tube 'megaprimer' PCR method
    • DOI 10.1093/nar/25.16.3371
    • Ke, S.H. and Madison, E.L. (1997) Rapid and efficient site-directed mutagenesis by single-tube 'megaprimer' PCR method. Nucleic Acids Res. 25, 3371-3372 (Pubitemid 27338700)
    • (1997) Nucleic Acids Research , vol.25 , Issue.16 , pp. 3371-3372
    • Ke, S.-H.1    Madison, E.L.2
  • 18
    • 0000243829 scopus 로고
    • PROCHEK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., Macarthur, M.W., Moss, D.S., and Thornton, J.M. (1993) PROCHEK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 19
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L. and Rosenström, P. (2010) Dali server: conservation mapping in 3D. Nucleic Acid Res. 38, 545-549
    • (2010) Nucleic Acid Res. , vol.38 , pp. 545-549
    • Holm, L.1    Rosenström, P.2
  • 20
    • 33846990432 scopus 로고    scopus 로고
    • Clavulanic acid dehydrogenase: Structural and biochemical analysis of the final step in the biosynthesis of the b-lactamase inhibitor clavulanic acid
    • Alasdair, K.M., Nadia, J.K., Helena, H., Carol, V.R., Christopher, J.S., Christopher, J.S., and Inger, A. (2007) Clavulanic acid dehydrogenase: structural and biochemical analysis of the final step in the biosynthesis of the b-lactamase inhibitor clavulanic acid. Biochemistry 46, 1523-1533
    • (2007) Biochemistry , vol.46 , pp. 1523-1533
    • Alasdair, K.M.1    Nadia, J.K.2    Helena, H.3    Carol, V.R.4    Christopher, J.S.5    Christopher, J.S.6    Inger, A.7
  • 21
    • 1542602992 scopus 로고    scopus 로고
    • Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG
    • DOI 10.1016/j.str.2004.02.008, PII S0969212604000504
    • Prince, A.C., Zhang, Y.M., Rock, C.O., and White, S.W. (2004) Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG. Structure 12, 417-428 (Pubitemid 38353063)
    • (2004) Structure , vol.12 , Issue.3 , pp. 417-428
    • Price, A.C.1    Zhang, Y.-M.2    Rock, C.O.3    White, S.W.4
  • 22
    • 0030586820 scopus 로고    scopus 로고
    • + identifies two principal targets for the design of inhibitors
    • DOI 10.1016/S0969-2126(96)00098-6
    • Breton, R., Housset, D., Mazza, C., and Fontecilla- Camps, J.C. (1996) The structure of a complex of human 17beta-hydroxysteroid dehydrogenase with estradiol and NADP' identifies two principal targets for the design of inhibitors. Structure 4, 905-915 (Pubitemid 26324703)
    • (1996) Structure , vol.4 , Issue.8 , pp. 905-915
    • Breton, R.1    Housset, D.2    Mazza, C.3    Fontecilla-Camps, J.C.4
  • 23
    • 25444447367 scopus 로고    scopus 로고
    • GASH: An improved algorithm formaximizing the number of equivalent residues between two protein structures
    • Standley, D.M., Toh, H., and Nakamura, H. (2005) GASH: an improved algorithm formaximizing the number of equivalent residues between two protein structures. BMC Bioinformatics 6, 221
    • (2005) BMC Bioinformatics , vol.6 , pp. 221
    • Standley, D.M.1    Toh, H.2    Nakamura, H.3
  • 24
    • 0000243829 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. Crystallogr. 26, 283-291
    • (1991) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Kraulis, P.J.1
  • 25
    • 0038243196 scopus 로고    scopus 로고
    • POVScript': A program for model and data visualization using persistence of Vision ray-tracing
    • Fenn, T.D., Ring, D., and Petsko, G.A. (2003) POVScript' : a program for model and data visualization using persistence of Vision ray-tracing. J. Appl. Crystallogr. 26, 944-947
    • (2003) J. Appl. Crystallogr. , vol.26 , pp. 944-947
    • Fenn, T.D.1    Ring, D.2    Petsko, G.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.