2ify
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2ify.jpg|left|200px]] | [[Image:2ify.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2ify", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_2ify| PDB=2ify | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Structure of Bacillus anthracis cofactor-independent phosphoglucerate mutase''' | '''Structure of Bacillus anthracis cofactor-independent phosphoglucerate mutase''' | ||
| Line 29: | Line 26: | ||
[[Category: Littlejohn, J E.]] | [[Category: Littlejohn, J E.]] | ||
[[Category: Nukui, M.]] | [[Category: Nukui, M.]] | ||
| - | [[Category: | + | [[Category: Bacillus anthracis]] |
| - | [[Category: | + | [[Category: Catalysis]] |
| - | [[Category: | + | [[Category: Catalytic mechanism]] |
| - | [[Category: | + | [[Category: Glygolysis]] |
| - | [[Category: | + | [[Category: Gram-posotive bacteria]] |
| - | [[Category: | + | [[Category: Phosphoglycerate]] |
| - | [[Category: | + | [[Category: Spore]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:27:30 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 04:27, 4 May 2008
Structure of Bacillus anthracis cofactor-independent phosphoglucerate mutase
Overview
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.
About this Structure
2IFY is a Single protein structure of sequence from Bacillus anthracis. Full crystallographic information is available from OCA.
Reference
Structure and molecular mechanism of Bacillus anthracis cofactor-independent phosphoglycerate mutase: a crucial enzyme for spores and growing cells of Bacillus species., Nukui M, Mello LV, Littlejohn JE, Setlow B, Setlow P, Kim K, Leighton T, Jedrzejas MJ, Biophys J. 2007 Feb 1;92(3):977-88. Epub 2006 Nov 3. PMID:17085493 Page seeded by OCA on Sun May 4 07:27:30 2008
