This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1c14
From Proteopedia
|
CRYSTAL STRUCTURE OF E COLI ENOYL REDUCTASE-NAD+-TRICLOSAN COMPLEX
Overview
The 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.
About this Structure
1C14 is a Single protein structure of sequence from Escherichia coli with NAD and TCL as ligands. Active as [acyl-carrier-protein_reductase_(NADH) Enoyl-[acyl-carrier-protein] reductase (NADH)], with EC number 1.3.1.9 Full crystallographic information is available from OCA.
Reference
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 [[Category: Enoyl-[acyl-carrier-protein] reductase (NADH)]]
Page seeded by OCA on Tue Nov 20 12:04:27 2007
Categories: Escherichia coli | Single protein | Abdel-Meguid, S. | Court, R. | Janson, C. | Payne, D. | Qiu, X. | Smyth, M. | NAD | TCL | Enoyl reductase | Fabi | Oxidoreductase | Triclosan
