2EX2

Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli

2EX2 の概要

• エントリーDOI: 10.2210/pdb2ex2/pdb
• 関連するPDBエントリー: 2EX6 2EX8 2EX9 2EXA 2EXB
• 分子名称: Penicillin-binding protein 4, GLYCEROL (3 entities in total)
• 機能のキーワード: penicillin-binding protein, penicillin, cephem, penem, d-alanyl-d-alanine-carboxypeptidase, d-alanyl-d-alanine-endopeptidase, hydrolase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm : P24228
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 49888.81

構造登録者

Kishida, H.,Unzai, S.,Roper, D.I.,Lloyd, A.,Park, S.-Y.,Tame, J.R.H. (登録日: 2005-11-07, 公開日: 2006-06-13, 最終更新日: 2024-10-30)

主引用文献

Kishida, H.,Unzai, S.,Roper, D.I.,Lloyd, A.,Park, S.-Y.,Tame, J.R.H.
Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics
Biochemistry, 45:783-792, 2006

PubMed 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.

PubMed: 16411754
DOI: 10.1021/bi051533t

実験手法

X-RAY DIFFRACTION (1.55 Å)