2ex6
From Proteopedia
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Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, complexed with ampicillin
Overview
The crystal structure of penicillin binding protein 4 (PBP4) from, Escherichia coli, which has both DD-endopeptidase and DD-carboxypeptidase, activity, is presented. PBP4 is one of 12 penicillin binding proteins in, E. coli involved in the synthesis and maintenance of the cell wall. The, model contains a penicillin binding domain similar to known structures, but includes a large insertion which folds into domains with unique folds., The structures of the protein covalently attached to five different, antibiotics presented here show the active site residues are unmoved, compared to the apoprotein, but nearby surface loops and helices are, displaced in some cases. The altered geometry of conserved active site, residues compared with those of other PBPs suggests a possible cause for, the slow deacylation rate of PBP4.
About this Structure
2EX6 is a Single protein structure of sequence from Escherichia coli with AIC and GOL as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics., Kishida H, Unzai S, Roper DI, Lloyd A, Park SY, Tame JR, Biochemistry. 2006 Jan 24;45(3):783-92. PMID:16411754
Page seeded by OCA on Wed Nov 21 10:12:01 2007
