Structural highlights
Function
[PDXH_MYCTU] Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP) (By similarity).[HAMAP-Rule:MF_01629]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of a putative pyridoxine 5'-phosphate oxidase (Rv2607) from Mycobacterium tuberculosis.,Pedelacq JD, Rho BS, Kim CY, Waldo GS, Lekin TP, Segelke BW, Rupp B, Hung LW, Kim SI, Terwilliger TC Proteins. 2006 Mar 15;62(3):563-9. PMID:16374842[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pedelacq JD, Rho BS, Kim CY, Waldo GS, Lekin TP, Segelke BW, Rupp B, Hung LW, Kim SI, Terwilliger TC. Crystal structure of a putative pyridoxine 5'-phosphate oxidase (Rv2607) from Mycobacterium tuberculosis. Proteins. 2006 Mar 15;62(3):563-9. PMID:16374842 doi:10.1002/prot.20824
