2f9y

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{{STRUCTURE_2f9y| PDB=2f9y | SCENE= }}
{{STRUCTURE_2f9y| PDB=2f9y | SCENE= }}
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'''The Crystal Structure of The Carboxyltransferase Subunit of ACC from Escherichia coli'''
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===The Crystal Structure of The Carboxyltransferase Subunit of ACC from Escherichia coli===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_16460018}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16460018 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16460018}}
==About this Structure==
==About this Structure==
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[[Category: Spiral domain]]
[[Category: Spiral domain]]
[[Category: Zinc ribbon]]
[[Category: Zinc ribbon]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:38:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:20:56 2008''

Revision as of 13:21, 29 July 2008

Image:2f9y.png

Template:STRUCTURE 2f9y

The Crystal Structure of The Carboxyltransferase Subunit of ACC from Escherichia coli

Template:ABSTRACT PUBMED 16460018

About this Structure

2F9Y is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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

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