2IFY
Structure of Bacillus anthracis cofactor-independent phosphoglucerate mutase
Summary for 2IFY
| Entry DOI | 10.2210/pdb2ify/pdb |
| Descriptor | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, MANGANESE (II) ION (3 entities in total) |
| Functional Keywords | catalysis, glygolysis, gram-posotive bacteria, spores, catalytic mechanism, phosphoglycerate, bacillus anthracis, isomerase |
| Biological source | Bacillus anthracis |
| Total number of polymer chains | 1 |
| Total formula weight | 56323.00 |
| Authors | Nukui, M.,Littlejohn, J.E.,Jedrzejas, M.J. (deposition date: 2006-09-21, release date: 2006-10-24, Last modification date: 2024-02-21) |
| Primary citation | Nukui, M.,Mello, L.V.,Littlejohn, J.E.,Setlow, B.,Setlow, P.,Kim, K.,Leighton, T.,Jedrzejas, M.J. Structure and Molecular Mechanism of Bacillus anthracis Cofactor-Independent Phosphoglycerate Mutase: A Crucial Enzyme for Spores and Growing Cells of Bacillus Species. Biophys.J., 92:977-988, 2007 Cited by PubMed Abstract: Phosphoglycerate mutases (PGMs) catalyze the isomerization of 2- and 3-phosphoglycerates and are essential for glucose metabolism in most organisms. This study reports the production, structure, and molecular dynamics analysis of Bacillus anthracis cofactor-independent PGM (iPGM). The three-dimensional structure of B. anthracis PGM is composed of two structural and functional domains, the phosphatase and transferase. The structural relationship between these two domains is different than in the B. stearothermophilus iPGM structure determined previously. However, the structures of the two domains of B. anthracis iPGM show a high degree of similarity to those in B. stearothermophilus iPGM. The novel domain arrangement in B. anthracis iPGM and the dynamic property of these domains is directly linked to the mechanism of enzyme catalysis, in which substrate binding is proposed to result in close association of the two domains. The structure of B. anthracis iPGM and the molecular dynamics of this structure provide unique insight into the mechanism of iPGM catalysis, in particular the roles of changes in coordination geometry of the enzyme's two bivalent metal ions and the regulation of this enzyme's activity by changes in intracellular pH during spore formation and germination in Bacillus species. PubMed: 17085493DOI: 10.1529/biophysj.106.093872 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.38 Å) |
Structure validation
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