2f9i | pdb_00002f9i
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 with ZN as ligand. 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 Tue Jan 29 19:31:15 2008
