1rii
Crystal structure of phosphoglycerate mutase from M. TuberculosisCrystal structure of phosphoglycerate mutase from M. Tuberculosis
Structural highlights
FunctionGPMA_MYCTU Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate (By similarity). Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe single-crystal X-ray structure of phosphoglycerate mutase from Mycobacterium tuberculosis has been determined at a resolution of 1.70 angstroms. The C-terminal tail of each of the subunits is flexible and disordered; however, for one of the four chains (chain A) all but five residues of the chain could be modeled. Noteworthy features of the structure include the active site and a proline-rich segment in each monomer forming a short left-handed polyprolyl helix. These segments lie on the enzyme surface and could conceivably participate in protein-protein interactions. The 1.70 angstroms X-ray crystal structure of Mycobacterium tuberculosis phosphoglycerate mutase.,Muller P, Sawaya MR, Pashkov I, Chan S, Nguyen C, Wu Y, Perry LJ, Eisenberg D Acta Crystallogr D Biol Crystallogr. 2005 Mar;61(Pt 3):309-15. Epub 2005, Feb 24. PMID:15735341[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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