Crystal Structure of Penicillin Binding Protein 4 (dacB) from Escherichia coli, both in the Native Form and Covalently Linked to Various Antibiotics

• DOI: 10.1021/bi051533t
• Publication Date: 2006-01-17T05:33:47Z
• Authors: Hiroyuki Kishida; Satoru Unzai; David I. Roper; Adrian Lloyd; Sam-Yong Park; Jeremy R. H. Tame
• Keywords: Penicillin binding proteins

The crystal structure of penicillin binding protein 4 (PBP4) from Escherichia coli, which has both DD-endopeptidase and DD-carboxypeptidase activity, is presented. PBP4 one 12 proteins in E. coli involved the synthesis maintenance cell wall. model contains a domain similar to known structures, but includes large insertion folds into domains with unique folds. structures covalently attached five different antibiotics presented here show active site residues are unmoved compared apoprotein, nearby surface loops helices displaced some cases. altered geometry conserved those other PBPs suggests possible cause for slow deacylation rate PBP4.