2f9i
From Proteopedia
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|PDB= 2f9i |SIZE=350|CAPTION= <scene name='initialview01'>2f9i</scene>, resolution 1.980Å | |PDB= 2f9i |SIZE=350|CAPTION= <scene name='initialview01'>2f9i</scene>, resolution 1.980Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= ACCA,ACCD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]) | |GENE= ACCA,ACCD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2f9y|2F9Y]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f9i OCA], [http://www.ebi.ac.uk/pdbsum/2f9i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f9i RCSB]</span> | ||
}} | }} | ||
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[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
[[Category: Bilder, P W.]] | [[Category: Bilder, P W.]] | ||
| - | [[Category: ZN]] | ||
[[Category: crotonase superfamily]] | [[Category: crotonase superfamily]] | ||
[[Category: spiral domain]] | [[Category: spiral domain]] | ||
[[Category: zinc ribbon]] | [[Category: zinc ribbon]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:59:48 2008'' |
Revision as of 23:59, 30 March 2008
| |||||||
| , resolution 1.980Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | ACCA,ACCD (Staphylococcus aureus) | ||||||
| Related: | 2F9Y
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About this Structure
2F9I is a Protein complex structure of sequences from Staphylococcus aureus. 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
Page seeded by OCA on Mon Mar 31 02:59:48 2008
