2h3g
From Proteopedia
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'''Structure of the Type III Pantothenate Kinase (CoaX) from Bacillus Anthracis''' | '''Structure of the Type III Pantothenate Kinase (CoaX) from Bacillus Anthracis''' | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Nicely, N I.]] | [[Category: Nicely, N I.]] | ||
| - | [[Category: | + | [[Category: Anthrax]] |
| - | [[Category: | + | [[Category: Askha]] |
| - | [[Category: | + | [[Category: Bacillus anthracis]] |
| - | [[Category: | + | [[Category: Coaa]] |
| - | [[Category: | + | [[Category: Coax]] |
| - | [[Category: | + | [[Category: Pantothenate kinase]] |
| - | [[Category: | + | [[Category: Type iii pantothenate kinase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:49:18 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 02:49, 4 May 2008
Structure of the Type III Pantothenate Kinase (CoaX) from Bacillus Anthracis
Overview
Coenzyme A (CoASH) is the major low-molecular weight thiol in Staphylococcus aureus and a number of other bacteria; the crystal structure of the S. aureus coenzyme A-disulfide reductase (CoADR), which maintains the reduced intracellular state of CoASH, has recently been reported [Mallett, T.C., Wallen, J.R., Karplus, P.A., Sakai, H., Tsukihara, T., and Claiborne, A. (2006) Biochemistry 45, 11278-89]. In this report we demonstrate that CoASH is the major thiol in Bacillus anthracis; a bioinformatics analysis indicates that three of the four proteins responsible for the conversion of pantothenate (Pan) to CoASH in Escherichia coli are conserved in B. anthracis. In contrast, a novel type III pantothenate kinase (PanK) catalyzes the first committed step in the biosynthetic pathway in B. anthracis; unlike the E. coli type I PanK, this enzyme is not subject to feedback inhibition by CoASH. The crystal structure of B. anthracis PanK (BaPanK), solved using multiwavelength anomalous dispersion data and refined at a resolution of 2.0 A, demonstrates that BaPanK is a new member of the Acetate and Sugar Kinase/Hsc70/Actin (ASKHA) superfamily. The Pan and ATP substrates have been modeled into the active-site cleft; in addition to providing a clear rationale for the absence of CoASH inhibition, analysis of the Pan-binding pocket has led to the development of two new structure-based motifs (the PAN and INTERFACE motifs). Our analyses also suggest that the type III PanK in the spore-forming B. anthracis plays an essential role in the novel thiol/disulfide redox biology of this category A biodefense pathogen.
About this Structure
2H3G is a Single protein structure of sequence from Bacillus anthracis. Full crystallographic information is available from OCA.
Reference
Structure of the type III pantothenate kinase from Bacillus anthracis at 2.0 A resolution: implications for coenzyme A-dependent redox biology., Nicely NI, Parsonage D, Paige C, Newton GL, Fahey RC, Leonardi R, Jackowski S, Mallett TC, Claiborne A, Biochemistry. 2007 Mar 20;46(11):3234-45. Epub 2007 Feb 27. PMID:17323930 Page seeded by OCA on Sun May 4 05:49:18 2008
