4OX3

Structure of the LdcB LD-carboxypeptidase reveals the molecular basis of peptidoglycan recognition

4OX3 の概要

• エントリーDOI: 10.2210/pdb4ox3/pdb
• 関連するPDBエントリー: 4OX5 4OXD
• 分子名称: Putative carboxypeptidase YodJ, ZINC ION, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: las family, ld-carboxypeptidase, cell wall modifying enzyme, hydrolase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25423.70

構造登録者

Hoyland, C.N.,Aldridge, C.,Cleverley, R.M.,Sidiq, K.,Duchene, M.C.,Daniel, R.A.,Vollmer, W.,Lewis, R.J. (登録日: 2014-02-04, 公開日: 2014-06-11, 最終更新日: 2023-12-27)

主引用文献

Hoyland, C.N.,Aldridge, C.,Cleverley, R.M.,Duchene, M.C.,Minasov, G.,Onopriyenko, O.,Sidiq, K.,Stogios, P.J.,Anderson, W.F.,Daniel, R.A.,Savchenko, A.,Vollmer, W.,Lewis, R.J.
Structure of the LdcB LD-carboxypeptidase reveals the molecular basis of peptidoglycan recognition.
Structure, 22:949-960, 2014

PubMed Abstract: Peptidoglycan surrounds the bacterial cytoplasmic membrane to protect the cell against osmolysis. The biosynthesis of peptidoglycan, made of glycan strands crosslinked by short peptides, is the target of antibiotics like β-lactams and glycopeptides. Nascent peptidoglycan contains pentapeptides that are trimmed by carboxypeptidases to tetra- and tripeptides. The well-characterized DD-carboxypeptidases hydrolyze the terminal D-alanine from the stem pentapeptide to produce a tetrapeptide. However, few LD-carboxypeptidases that produce tripeptides have been identified, and nothing is known about substrate specificity in these enzymes. We report biochemical properties and crystal structures of the LD-carboxypeptidases LdcB from Streptococcus pneumoniae, Bacillus anthracis, and Bacillus subtilis. The enzymes are active against bacterial cell wall tetrapeptides and adopt a zinc-carboxypeptidase fold characteristic of the LAS superfamily. We have also solved the structure of S. pneumoniae LdcB with a product mimic, elucidating the residues essential for peptidoglycan recognition and the conformational changes that occur on ligand binding.

PubMed: 24909784
DOI: 10.1016/j.str.2014.04.015

実験手法

X-RAY DIFFRACTION (2 Å)