2F9Y

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

Summary for 2F9Y

• Entry DOI: 10.2210/pdb2f9y/pdb
• Related: 2F9I
• Descriptor: Acetyl-CoA carboxylase, Carboxyltransferase alpha chain, Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, ZINC ION, ... (4 entities in total)
• Functional Keywords: zinc ribbon, crotonase superfamily, spiral domain, ligase
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm : P0A9Q6
• Total number of polymer chains: 2
• Total formula weight: 70932.26

Authors

Bilder, P.W. (deposition date: 2005-12-06, release date: 2006-12-12, Last modification date: 2024-10-16)

Primary citation

Bilder, P.,Lightle, S.,Bainbridge, G.,Ohren, J.,Finzel, B.,Sun, F.,Holley, S.,Al-Kassim, L.,Spessard, C.,Melnick, M.,Newcomer, M.,Waldrop, G.L.
The Structure of the Carboxyltransferase Component of Acetyl-CoA Carboxylase Reveals a Zinc-Binding Motif Unique to the Bacterial Enzyme(,).
Biochemistry, 45:1712-1722, 2006

PubMed Abstract: 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.

PubMed: 16460018
DOI: 10.1021/bi0520479

Experimental method

X-RAY DIFFRACTION (3.2 Å)