The Structure of the Carboxyltransferase Component of Acetyl-CoA Carboxylase Reveals a Zinc-Binding Motif Unique to the Bacterial Enzyme, | Zendy

P.W. Bilder | Zendy; Sandra Lightle | Zendy; Graeme Bainbridge | Zendy; Jeffrey F. Ohren | Zendy; B.C. Finzel | Zendy; Fang Sun | Zendy; Susan Holley | Zendy; Loola S. Al-Kassim | Zendy; Cindy Spessard | Zendy; Michael Melnick | Zendy; Marcia E. Newcomer | Zendy; Grover L. Waldrop | Zendy

Open Access

The Structure of the Carboxyltransferase Component of Acetyl-CoA Carboxylase Reveals a Zinc-Binding Motif Unique to the Bacterial Enzyme^,

Author(s) -

P.W. Bilder,

Sandra Lightle,

Graeme Bainbridge,

Jeffrey F. Ohren,

B.C. Finzel,

Fang Sun,

Susan Holley,

Loola S. Al-Kassim,

Cindy Spessard,

Michael Melnick,

Marcia E. Newcomer,

Grover L. Waldrop

Publication year - 2006

Publication title -

biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.43

H-Index - 253

eISSN - 1520-4995

pISSN - 0006-2960

DOI - 10.1021/bi0520479

Subject(s) - biochemistry , pyruvate carboxylase , enzyme , acetyl coa carboxylase , protein subunit , escherichia coli , biotin , chemistry , fatty acid synthesis , biology , gene

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.

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