Kishida, H., Unzai, Satoru, Roper, David I., Lloyd, A, Park, S.Y. and Tame, Jeremy R. H. (2006) Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics. Biochemistry, Vol.45 (No.3). pp. 783-792. doi:10.1021/bi051533t

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Abstract

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.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry
Divisions:	Faculty of Science > Life Sciences (2010- )
Journal or Publication Title:	Biochemistry
Publisher:	American Chemical Society
ISSN:	0006-2960
Official Date:	24 January 2006
Dates:	Date Event 24 January 2006 Published
Volume:	Vol.45
Number:	No.3
Number of Pages:	10
Page Range:	pp. 783-792
DOI:	10.1021/bi051533t
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access

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