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

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

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

Qingping Xu,Kumar Singh Saikatendu,S Sri Krishna,Daniel McMullan,Polat Abdubek,Sanjay Agarwalla,Eileen Ambing,Tamara Astakhova,Herbert L Axelrod,Dennis Carlton,Hsiu-Ju Chiu,Thomas Clayton,Michael DiDonato,Lian Duan, Elsliger,Julie Feuerhelm,Slawomir K Grzechnik,Joanna Hale,Eric Hampton,Gye Won Han,Justin Haugen,Lukasz Jaroszewski,Kevin K Jin,Heath E Klock,Mark W Knuth,Eric Koesema,Mitchell D Miller,Andrew T Morse,Edward Nigoghossian,Linda Okach,Silvya Oommachen,Jessica Paulsen,Ron Reyes,Christopher L Rife,Robert Schwarzenbacher,Henry van den Bedem,Aprilfawn White,Guenter Wolf,Keith O Hodgson,John Wooley,Ashley M Deacon,Adam Godzik,Scott A Lesley,Ian A Wilson,

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

Q Xu,KS Saikatendu,SS Krishna,D McMullan,P Abdubek,S Agarwalla,E Ambing,T Astakhova,HL Axelrod,D Carlton,HJ Chiu,T Clayton,M DiDonato,L Duan,MA Elsliger,J Feuerhelm,SK Grzechnik,J Hale,E Hampton,GW Han,J Haugen,L Jaroszewski,KK Jin,HE Klock,MW Knuth,E Koesema,MD Miller,AT Morse,E Nigoghossian,L Okach,S Oommachen,J Paulsen,R Reyes,CL Rife,R Schwarzenbacher,H van den Bedem,A White,G Wolf,KO Hodgson,J Wooley,AM Deacon,A Godzik,SA Lesley,IA Wilson,

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

PUBLICATION TYPE: Validation Studies

Journal: Proteins

VOLUME: 69

Page Numbers: 433-9

Journal Abbreviation: Proteins

ISSN: 1097-0134

DAY: 1

MONTH: Nov

YEAR: 2007

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

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LANGUAGE: eng

NlmUniqueID: 8700181

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

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

AFFILIATION: Stanford Synchrotron Radiation Laboratory, Stanford University, Menlo Park, California, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: U54 GM074898

ACRONYM: GM

MEDLINETA: Proteins

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