2f9y
From Proteopedia
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|PDB= 2f9y |SIZE=350|CAPTION= <scene name='initialview01'>2f9y</scene>, resolution 3.20Å | |PDB= 2f9y |SIZE=350|CAPTION= <scene name='initialview01'>2f9y</scene>, resolution 3.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Acetyl-CoA_carboxylase Acetyl-CoA carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.2 6.4.1.2] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_carboxylase Acetyl-CoA carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.2 6.4.1.2] </span> |
|GENE= accD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= accD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2f9i|2F9I]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f9y OCA], [http://www.ebi.ac.uk/pdbsum/2f9y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f9y RCSB]</span> | ||
}} | }} | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[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 02:59:55 2008'' |
Revision as of 23:59, 30 March 2008
| |||||||
| , resolution 3.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | accD (Escherichia coli) | ||||||
| Activity: | Acetyl-CoA carboxylase, with EC number 6.4.1.2 | ||||||
| Related: | 2F9I
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The Crystal Structure of The Carboxyltransferase Subunit of ACC from Escherichia coli
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
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
Page seeded by OCA on Mon Mar 31 02:59:55 2008
