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Volumn 69, Issue 2, 2007, Pages 433-439

Crystal structure of MtnX phosphatase from Bacillus subtilis at 2.0 Å resolution provides a structural basis for bipartite phosphomonoester hydrolysis of 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate

(44)  Xu, Qingping a,b   Saikatendu, Kumar Singh c   Sri Krishna, S a,d,e   McMullan, Daniel a,f   Abdubek, Polat a,f   Agarwalla, Sanjay a,f   Ambing, Eileen a,f   Astakhova, Tamara a,e   Axelrod, Herbert L a,b   Carlton, Dennis a,c   Chiu, Hsiu Ju a,b   Clayton, Thomas a,c   DiDonato, Michael a,f   Duan, Lian a,e   Elsliger, Marc André a,c   Feuerhelm, Julie a,f   Grzechnik, Slawomir K a,e   Hale, Joanna a,f   Hampton, Eric a,f   Gye, Won Han a,c   more..


Author keywords

[No Author keywords available]

Indexed keywords

2 HYDROXY 3 KETO 5 METHYLTHIOPENTENYL 1 PHOSPHATE; BACTERIAL ENZYME; MTNX PHOSPHATASE; PHOSPHOMONOESTER DERIVATIVE; PHOSPHORUS DERIVATIVE; UNCLASSIFIED DRUG;

EID: 34548707083     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21602     Document Type: Article
Times cited : (6)

References (32)
  • 3
    • 0033028593 scopus 로고    scopus 로고
    • Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae
    • Heilbronn J, Wilson J, Berger BJ. Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae. J Bacteriol 1999;181:1739-1747.
    • (1999) J Bacteriol , vol.181 , pp. 1739-1747
    • Heilbronn, J.1    Wilson, J.2    Berger, B.J.3
  • 4
    • 0022412459 scopus 로고
    • The metabolism of 5′-methylthioadenosine and 5-methylthioribose 1-phosphate in Saccharomyces cerevisiae
    • Marchitto KS, Ferro AJ. The metabolism of 5′-methylthioadenosine and 5-methylthioribose 1-phosphate in Saccharomyces cerevisiae. J Gen Microbiol 1985;131:2153-2164.
    • (1985) J Gen Microbiol , vol.131 , pp. 2153-2164
    • Marchitto, K.S.1    Ferro, A.J.2
  • 5
    • 0023791057 scopus 로고
    • Analogs of 5-methylthioribose, a novel class of antiprotozoal agents
    • Riscoe MK, Ferro AJ, Fitchen JH. Analogs of 5-methylthioribose, a novel class of antiprotozoal agents. Antimicrob Agents Chemother 1988;32:1904-1906.
    • (1988) Antimicrob Agents Chemother , vol.32 , pp. 1904-1906
    • Riscoe, M.K.1    Ferro, A.J.2    Fitchen, J.H.3
  • 9
    • 0036896410 scopus 로고    scopus 로고
    • An automated system to mount cryo-cooled protein crystals on a synchrotron beamline, using compact sample cassettes and a small-scale robot
    • Cohen AE, Ellis PJ, Miller MD, Deacon AM, Phizackerley RP. An automated system to mount cryo-cooled protein crystals on a synchrotron beamline, using compact sample cassettes and a small-scale robot. J Appl Crystallogr 2002;35:720-726.
    • (2002) J Appl Crystallogr , vol.35 , pp. 720-726
    • Cohen, A.E.1    Ellis, P.J.2    Miller, M.D.3    Deacon, A.M.4    Phizackerley, R.P.5
  • 10
    • 0028103275 scopus 로고    scopus 로고
    • The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50:760-763.
    • The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50:760-763.
  • 11
    • 0032031476 scopus 로고    scopus 로고
    • Error estimates of protein structure coordinates and deviations from standard geometry by full-matrix refinement of gammaB- and betaB2-crystallin
    • Tickle IJ, Laskowski RA, Moss DS. Error estimates of protein structure coordinates and deviations from standard geometry by full-matrix refinement of gammaB- and betaB2-crystallin. Acta Crystallogr D Biol Crystallogr 1998;54:243-252.
    • (1998) Acta Crystallogr D Biol Crystallogr , vol.54 , pp. 243-252
    • Tickle, I.J.1    Laskowski, R.A.2    Moss, D.S.3
  • 15
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A, Morris R, Lamzin VS. Automated protein model building combined with iterative structure refinement. Nat Struct Biol 1999;6:458-463.
    • (1999) Nat Struct Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 16
  • 18
    • 3242886389 scopus 로고    scopus 로고
    • MOLPROBITY: Structure validation and all-atom contact analysis for nucleic acids and their complexes
    • Davis IW, Murray LW, Richardson JS, Richardson DC. MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes. Nucleic Acids Res 2004;32:W615-W619.
    • (2004) Nucleic Acids Res , vol.32
    • Davis, I.W.1    Murray, L.W.2    Richardson, J.S.3    Richardson, D.C.4
  • 19
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine AA, Richelle J, Wodak SJ. SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr D Biol Crystallogr 1999;55:191-205.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 20
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program. J Mol Graph
    • 29
    • Vriend G. WHAT IF: a molecular modeling and drug design program. J Mol Graph 1990;8:52-56, 29.
    • (1990) , vol.8 , pp. 52-56
    • Vriend, G.1
  • 21
    • 0032169688 scopus 로고    scopus 로고
    • PQS: A protein quaternary structure file server
    • Henrick K, Thornton JM. PQS: a protein quaternary structure file server. Trends Biochem Sci 1998;23:358-361.
    • (1998) Trends Biochem Sci , vol.23 , pp. 358-361
    • Henrick, K.1    Thornton, J.M.2
  • 22
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW. Solvent content of protein crystals. J Mol Biol 1968;33:491-497.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 23
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, Chothia C. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 1995;247:536-540.
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 24
    • 0028871926 scopus 로고
    • Dali: A network tool for protein structure comparison
    • Holm L, Sander C. Dali: a network tool for protein structure comparison. Trends Biochem Sci 1995;20:478-480.
    • (1995) Trends Biochem Sci , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 25
    • 0036301579 scopus 로고    scopus 로고
    • Structural characterization of the reaction pathway in phosphoserine phosphatase: Crystallographic "snapshots" of intermediate states
    • Wang W, Cho HS, Kim R, Jancarik J, Yokota H, Nguyen HH, Grigoriev IV, Wemmer DE, Kim SH. Structural characterization of the reaction pathway in phosphoserine phosphatase: crystallographic "snapshots" of intermediate states. J Mol Biol 2002;319:421-431.
    • (2002) J Mol Biol , vol.319 , pp. 421-431
    • Wang, W.1    Cho, H.S.2    Kim, R.3    Jancarik, J.4    Yokota, H.5    Nguyen, H.H.6    Grigoriev, I.V.7    Wemmer, D.E.8    Kim, S.H.9
  • 26
    • 1842424658 scopus 로고    scopus 로고
    • The thrH gene product of Pseudomonas aeruginosa is a dual activity enzyme with a novel phosphoserine: Homoserine phosphotransferase activity
    • Singh SK, Yang K, Karthikeyan S, Huynh T, Zhang X, Phillips MA, Zhang H. The thrH gene product of Pseudomonas aeruginosa is a dual activity enzyme with a novel phosphoserine: homoserine phosphotransferase activity. J Biol Chem 2004;279:13166-13173.
    • (2004) J Biol Chem , vol.279 , pp. 13166-13173
    • Singh, S.K.1    Yang, K.2    Karthikeyan, S.3    Huynh, T.4    Zhang, X.5    Phillips, M.A.6    Zhang, H.7
  • 27
    • 0035902464 scopus 로고    scopus 로고
    • BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: Structure of a BeF(3)(-) complex with phosphoserine phosphatase
    • Cho H, Wang W, Kim R, Yokota H, Damo S, Kim SH, Wemmer D, Kustu S, Yan D. BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: structure of a BeF(3)(-) complex with phosphoserine phosphatase. Proc Natl Acad Sci USA 2001;98:8525-8530.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 8525-8530
    • Cho, H.1    Wang, W.2    Kim, R.3    Yokota, H.4    Damo, S.5    Kim, S.H.6    Wemmer, D.7    Kustu, S.8    Yan, D.9
  • 29
    • 0242585345 scopus 로고    scopus 로고
    • The pentacovalent phosphorus intermediate of a phosphoryl transfer reaction
    • Lahiri SD, Zhang G, Dunaway-Mariano D, Allen KN. The pentacovalent phosphorus intermediate of a phosphoryl transfer reaction. Science 2003;299:2067-2071.
    • (2003) Science , vol.299 , pp. 2067-2071
    • Lahiri, S.D.1    Zhang, G.2    Dunaway-Mariano, D.3    Allen, K.N.4
  • 30
    • 0033102133 scopus 로고    scopus 로고
    • Mechanistic alternatives in phosphate monoester hydrolysis: What conclusions can be drawn from available experimental data?
    • Aqvist J, Kolmodin K, Florian J, Warshel A. Mechanistic alternatives in phosphate monoester hydrolysis: what conclusions can be drawn from available experimental data? Chem Biol 1999;6:R71-R80.
    • (1999) Chem Biol , vol.6
    • Aqvist, J.1    Kolmodin, K.2    Florian, J.3    Warshel, A.4
  • 31
    • 17444387092 scopus 로고    scopus 로고
    • Crystal structure of human E1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase activity
    • Wang H, Pang H, Bartlam M, Rao Z. Crystal structure of human E1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase activity. J Mol Biol 2005;348:917-926.
    • (2005) J Mol Biol , vol.348 , pp. 917-926
    • Wang, H.1    Pang, H.2    Bartlam, M.3    Rao, Z.4
  • 32
    • 0037439997 scopus 로고    scopus 로고
    • Structural classification of zinc fingers: Survey and summary
    • Krishna SS, Majumdar I, Grishin NV. Structural classification of zinc fingers: survey and summary. Nucleic Acids Res 2003;31:532-550.
    • (2003) Nucleic Acids Res , vol.31 , pp. 532-550
    • Krishna, S.S.1    Majumdar, I.2    Grishin, N.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.