1RII

Crystal structure of phosphoglycerate mutase from M. Tuberculosis

Summary for 1RII

• Entry DOI: 10.2210/pdb1rii/pdb
• Descriptor: 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase, GLYCEROL (3 entities in total)
• Functional Keywords: phosphoglyerate mutase, sh3 domain binding, structural genomics, tbsgc, protein structure initiative, psi, tb structural genomics consortium, isomerase
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 4
• Total formula weight: 116459.18

Authors

Mueller, P.,Sawaya, M.R.,Chan, S.,Wu, Y.,Pashkova, I.,Perry, J.,Eisenberg, D.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2003-11-17, release date: 2004-10-05, Last modification date: 2023-08-23)

Primary citation

Muller, P.,Sawaya, M.R.,Pashkov, I.,Chan, S.,Nguyen, C.,Wu, Y.,Perry, L.J.,Eisenberg, D.
The 1.70 angstroms X-ray crystal structure of Mycobacterium tuberculosis phosphoglycerate mutase.
Acta Crystallogr.,Sect.D, 61:309-315, 2005

PubMed Abstract: The 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.

PubMed: 15735341
DOI: 10.1107/S0907444904033190

Experimental method

X-RAY DIFFRACTION (1.7 Å)