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1fte
From Proteopedia
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CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE ACYL CARRIER PROTEIN SYNTHASE (NATIVE 1)
Overview
Acyl carrier protein synthase (AcpS) catalyzes the formation of holo-ACP, which mediates the essential transfer of acyl fatty acid intermediates, during the biosynthesis of fatty acids and lipids in the cell. Thus, AcpS, plays an important role in bacterial fatty acid and lipid biosynthesis, making it an attractive target for therapeutic intervention. We have, determined, for the first time, the crystal structure of the Streptococcus, pneumoniae AcpS and AcpS complexed with 3'5'-ADP, a product of AcpS, at, 2.0 and 1.9 A resolution, respectively. The crystal structure reveals an, alpha/beta fold and shows that AcpS assembles as a tightly packed, functional trimer, with a non-crystallographic pseudo-symmetric 3-fold, axis, which contains three active sites at the interface between, protomers. Only two active sites are occupied by the ligand molecules., Although there is virtually no sequence similarity between the, S.pneumoniae AcpS and the Bacillus subtilis Sfp transferase, a striking, structural similarity between both enzymes was observed. These data, provide a starting point for structure-based drug design efforts towards, the identification of AcpS inhibitors with potent antibacterial activity.
About this Structure
1FTE is a Single protein structure of sequence from Streptococcus pneumoniae with SO4 as ligand. Active as [acyl-carrier-protein_synthase Holo-[acyl-carrier-protein] synthase], with EC number 2.7.8.7 Full crystallographic information is available from OCA.
Reference
Crystal structure of Streptococcus pneumoniae acyl carrier protein synthase: an essential enzyme in bacterial fatty acid biosynthesis., Chirgadze NY, Briggs SL, McAllister KA, Fischl AS, Zhao G, EMBO J. 2000 Oct 16;19(20):5281-7. PMID:11032795 [[Category: Holo-[acyl-carrier-protein] synthase]]
Page seeded by OCA on Tue Nov 20 15:15:35 2007
