This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2h3g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2h3g.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2h3g.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2h3g| PDB=2h3g | SCENE= }}
{{STRUCTURE_2h3g| PDB=2h3g | SCENE= }}
-
'''Structure of the Type III Pantothenate Kinase (CoaX) from Bacillus Anthracis'''
+
===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.
+
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.
 +
-->
 +
{{ABSTRACT_PUBMED_17323930}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[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

Image:2h3g.png

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2h3g"
Personal tools