2f9i: Difference between revisions

Revision as of 04:39, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2f9i.png

Template:STRUCTURE 2f9i

Crystal Structure of the carboxyltransferase subunit of ACC from Staphylococcus aureusCrystal Structure of the carboxyltransferase subunit of ACC from Staphylococcus aureus

Template:ABSTRACT PUBMED 16460018

About this StructureAbout this Structure

2F9I is a Protein complex structure of sequences from Staphylococcus aureus. Full crystallographic information is available from OCA.

ReferenceReference

The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme., Bilder P, Lightle S, Bainbridge G, Ohren J, Finzel B, Sun F, Holley S, Al-Kassim L, Spessard C, Melnick M, Newcomer M, Waldrop GL, Biochemistry. 2006 Feb 14;45(6):1712-22. PMID:16460018

Page seeded by OCA on Tue Jul 29 04:39:53 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure of the carboxyltransferase subunit of ACC from Staphylococcus aureus'''
+===Crystal Structure of the carboxyltransferase subunit of ACC from Staphylococcus aureus===
-==Overview==
+<!--
-Acetyl-coA carboxylase (ACC) is a central metabolic enzyme that catalyzes the committed step in fatty acid biosynthesis: biotin-dependent conversion of acetyl-coA to malonyl-coA. The bacterial carboxyltransferase (CT) subunit of ACC is a target for the design of novel therapeutics that combat severe, hospital-acquired infections resistant to the established classes of frontline antimicrobials. Here, we present the structures of the bacterial CT subunits from two prevalent nosocomial pathogens, Staphylococcus aureus and Escherichia coli, at a resolution of 2.0 and 3.0 A, respectively. Both structures reveal a small, independent zinc-binding domain that lacks a complement in the primary sequence or structure of the eukaryotic homologue.
+The line below this paragraph, {{ABSTRACT_PUBMED_16460018}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16460018 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16460018}}
 ==About this Structure==
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 [[Category: Spiral domain]]
 [[Category: Zinc ribbon]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:37:47 2008''
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