Abstract
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 A 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.
(c) 2005 Wiley-Liss, Inc.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / chemistry*
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Bacterial Proteins / metabolism
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Cloning, Molecular
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Conserved Sequence
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Crystallography, X-Ray
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Dimerization
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Escherichia coli Proteins / chemistry
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Escherichia coli Proteins / metabolism
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Models, Molecular
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Molecular Sequence Data
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Mycobacterium tuberculosis / enzymology*
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Mycobacterium tuberculosis / genetics
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Polymerase Chain Reaction
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Protein Folding
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Protein Structure, Secondary
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Pyridoxaminephosphate Oxidase / chemistry*
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Pyridoxaminephosphate Oxidase / genetics
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Pyridoxaminephosphate Oxidase / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Sequence Alignment
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Sequence Homology, Amino Acid
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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Recombinant Proteins
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Pyridoxaminephosphate Oxidase