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Crystal structure of a putative pyridoxine 5′‐phosphate oxidase (Rv2607) from Mycobacterium tuberculosis
Author(s) -
Pédelacq JeanDenis,
Rho BeomSeop,
Kim ChangYub,
Waldo Geoffrey S.,
Lekin Timothy P.,
Segelke Brent W.,
Rupp Bernhard,
Hung LiWei,
Kim SuIl,
Terwilliger Thomas C.
Publication year - 2005
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.20824
Subject(s) - flavin mononucleotide , pyridoxine , dimer , flavin group , crystallography , oxidase test , cofactor , chemistry , crystal structure , mycobacterium tuberculosis , flavin adenine dinucleotide , protein structure , resolution (logic) , biochemistry , enzyme , tuberculosis , medicine , organic chemistry , pathology , artificial intelligence , computer science
The three‐dimensional structure of Rv2607, a putative pyridoxine 5′‐phosphate oxidase (PNPOx) from Mycobacterium tuberculosis, has been determined by X‐ray crystallography to 2.5 Å resolution. Rv2607 has a core domain similar to known PNPOx structures with a flavin mononucleotide (FMN) cofactor. Electron density for two FMN at the dimer interface is weak despite the bright yellow color of the protein solution and crystal. The shape and size of the putative binding pocket is markedly different from that of members of the PNPOx family, which may indicate some significant changes in the FMN binding mode of this protein relative to members of the family. Proteins 2006. © 2005 Wiley‐Liss, Inc.