5Z01

Native Escherichia coli L,D-carboxypeptidase A (LdcA)

5Z01 の概要

• エントリーDOI: 10.2210/pdb5z01/pdb
• 分子名称: Murein tetrapeptide carboxypeptidase, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: peptidoglycan, recycling, cell-wall, hydrolase
• 由来する生物種: Escherichia coli (strain K12)
• 細胞内の位置: Cytoplasm : P76008
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35711.95

構造登録者

Meyer, K.,Tame, J.R.H. (登録日: 2017-12-18, 公開日: 2018-04-25, 最終更新日: 2024-03-27)

主引用文献

Meyer, K.,Addy, C.,Akashi, S.,Roper, D.I.,Tame, J.R.H.
The crystal structure and oligomeric form of Escherichia colil,d-carboxypeptidase A.
Biochem. Biophys. Res. Commun., 499:594-599, 2018

PubMed Abstract: Bacterial peptidoglycan is constructed by cross-linking sugar chains carrying pentapeptide building blocks with two d-alanine residues at the C-terminus. Incorporation into the polymer and subsequent breakdown of peptidoglycan releases a tetrapeptide with a single d-alanine residue. Removal of this residue is necessary for the tripeptide to receive a new D-Ala-D-Ala dipeptide in the synthetic pathway, but proteases are generally unable to work with substrates having residues of unusual chirality close to the scissile bond. Processing of the tetrapeptide is carried out by a dedicated ld-carboxypeptidase, which is of interest as a novel drug target. We describe the high resolution crystal structure of the enzyme from E. coli, and demonstrate the dimeric structure is highly conserved.

PubMed: 29601819
DOI: 10.1016/j.bbrc.2018.03.195

実験手法

X-RAY DIFFRACTION (1.75 Å)