1c14
From Proteopedia
CRYSTAL STRUCTURE OF E COLI ENOYL REDUCTASE-NAD+-TRICLOSAN COMPLEX
Structural highlights
Function[FABI_ECOLI] Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism and in the biotin biosynthesis.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of the Escherichia coli enoyl reductase-NAD+-triclosan complex has been determined at 2.5 A resolution. The Ile192-Ser198 loop is either disordered or in an open conformation in the previously reported structures of the enzyme. This loop adopts a closed conformation in our structure, forming van der Waals interactions with the inhibitor and hydrogen bonds with the bound NAD+ cofactor. The opening and closing of this flipping loop is likely an important factor in substrate or ligand recognition. The closed conformation of the loop appears to be a critical feature for the enhanced binding potency of triclosan, and a key component in future structure-based inhibitor design. Molecular basis for triclosan activity involves a flipping loop in the active site.,Qiu X, Janson CA, Court RI, Smyth MG, Payne DJ, Abdel-Meguid SS Protein Sci. 1999 Nov;8(11):2529-32. PMID:10595560[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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