1v35
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(New page: 200px<br /><applet load="1v35" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v35, resolution 2.50Å" /> '''Crystal Structure of...)
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Revision as of 02:25, 25 November 2007
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Crystal Structure of Eoyl-ACP Reductase with NADH
Overview
Bacteria synthesize fatty acids in a dissociated type pathway different, from that in humans. Enoyl acyl carrier protein reductase, which catalyzes, the final step of fatty acid elongation, has been validated as a potential, anti-microbial drug target. Triclosan is known to inhibit this enzyme, effectively. Precise characterization of the mode of triclosan binding is, required to develop highly specific inhibitors. With this in view, interactions between triclosan, the cofactor NADH/NAD+ and the enzyme from, five different species, one plant and four of microbial origin, have been, examined in the available crystal structures. A comparison of these, structures shows major structural differences at the, substrate/inhibitor/cofactor-binding loop. The analysis reveals that the, conformation of this flexible loop and the binding affinities of triclosan, to each of these enzymes are strongly correlated.
About this Structure
1V35 is a Single protein structure of sequence from Plasmodium falciparum with NAI as ligand. 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
Structural basis for the variation in triclosan affinity to enoyl reductases., Pidugu LS, Kapoor M, Surolia N, Surolia A, Suguna K, J Mol Biol. 2004 Oct 8;343(1):147-55. PMID:15381426 [[Category: Enoyl-[acyl-carrier-protein] reductase (NADH)]]
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