2ify
From Proteopedia
(New page: 200px<br /><applet load="2ify" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ify, resolution 2.38Å" /> '''Structure of Bacillu...) |
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| - | [[Image:2ify.jpg|left|200px]]<br /><applet load="2ify" size=" | + | [[Image:2ify.jpg|left|200px]]<br /><applet load="2ify" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ify, resolution 2.38Å" /> | caption="2ify, resolution 2.38Å" /> | ||
'''Structure of Bacillus anthracis cofactor-independent phosphoglucerate mutase'''<br /> | '''Structure of Bacillus anthracis cofactor-independent phosphoglucerate mutase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Phosphoglycerate mutases (PGMs) catalyze the isomerization of 2- and | + | 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== | ==About this Structure== | ||
| - | 2IFY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis] with MN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phosphoglycerate_mutase Phosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.1 5.4.2.1] Full crystallographic information is available from [http:// | + | 2IFY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis] with <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phosphoglycerate_mutase Phosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.1 5.4.2.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IFY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Phosphoglycerate mutase]] | [[Category: Phosphoglycerate mutase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Jedrzejas, M | + | [[Category: Jedrzejas, M J.]] |
| - | [[Category: Littlejohn, J | + | [[Category: Littlejohn, J E.]] |
[[Category: Nukui, M.]] | [[Category: Nukui, M.]] | ||
[[Category: MN]] | [[Category: MN]] | ||
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[[Category: spores]] | [[Category: spores]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:52:21 2008'' |
Revision as of 15:52, 21 February 2008
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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 with as ligand. Active as Phosphoglycerate mutase, with EC number 5.4.2.1 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
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