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| | {{STRUCTURE_2h3g| PDB=2h3g | SCENE= }} | | {{STRUCTURE_2h3g| PDB=2h3g | SCENE= }} |
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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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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17323930}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17323930 is the PubMed ID number. |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Pantothenate kinase]] | | [[Category: Pantothenate kinase]] |
| | [[Category: Type iii pantothenate kinase]] | | [[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 Tue Jul 29 13:39:31 2008'' |
Revision as of 10:39, 29 July 2008
Template:STRUCTURE 2h3g
Structure of the Type III Pantothenate Kinase (CoaX) from Bacillus Anthracis
Template:ABSTRACT PUBMED 17323930
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 Tue Jul 29 13:39:31 2008
