2f9i: Difference between revisions
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'''Crystal Structure of the carboxyltransferase subunit of ACC from Staphylococcus aureus''' | {{Structure | ||
|PDB= 2f9i |SIZE=350|CAPTION= <scene name='initialview01'>2f9i</scene>, resolution 1.980Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |||
|ACTIVITY= | |||
|GENE= ACCA,ACCD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]) | |||
}} | |||
'''Crystal Structure of the carboxyltransferase subunit of ACC from Staphylococcus aureus''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2F9I is a [ | 2F9I is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F9I OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16460018 16460018] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
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[[Category: zinc ribbon]] | [[Category: zinc ribbon]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:49:43 2008'' | ||
Revision as of 17:49, 20 March 2008
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| , resolution 1.980Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | ACCA,ACCD (Staphylococcus aureus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the carboxyltransferase subunit of ACC from Staphylococcus aureus
OverviewOverview
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 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
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