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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
Author(s) -
Xu Qingping,
Saikatendu Kumar Singh,
Krishna S. Sri,
McMullan Daniel,
Abdubek Polat,
Agarwalla Sanjay,
Ambing Eileen,
Astakhova Tamara,
Axelrod Herbert L.,
Carlton Dennis,
Chiu HsiuJu,
Clayton Thomas,
DiDonato Michael,
Duan Lian,
Elsliger MarcAndré,
Feuerhelm Julie,
Grzechnik Slawomir K.,
Hale Joanna,
Hampton Eric,
Han Gye Won,
Haugen Justin,
Jaroszewski Lukasz,
Jin Kevin K.,
Klock Heath E.,
Knuth Mark W.,
Koesema Eric,
Miller Mitchell D.,
Morse Andrew T.,
Nigoghossian Edward,
Okach Linda,
Oommachen Silvya,
Paulsen Jessica,
Reyes Ron,
Rife Christopher L.,
Schwarzenbacher Robert,
van den Bedem Henry,
White Aprilfawn,
Wolf Guenter,
Hodgson Keith O.,
Wooley John,
Deacon Ashley M.,
Godzik Adam,
Lesley Scott A.,
Wilson Ian A.
Publication year - 2007
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.21602
Subject(s) - bacillus subtilis , bipartite graph , hydrolysis , phosphate , resolution (logic) , phosphatase , chemistry , basis (linear algebra) , crystal (programming language) , biochemistry , combinatorics , biology , bacteria , enzyme , computer science , mathematics , genetics , artificial intelligence , graph , geometry , programming language
No abastract.