5KQB

Identification and structural characterization of LytU

5KQB の概要

• エントリーDOI: 10.2210/pdb5kqb/pdb
• NMR情報: BMRB: 30130
• 分子名称: Peptidase M23, ZINC ION (2 entities in total)
• 機能のキーワード: lysostaphin, lytu, peptidoglycan, zinc, hydrolase
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16337.54

構造登録者

Raulinaitis, V.,Tossavainen, H.,Permi, P. (登録日: 2016-07-06, 公開日: 2017-08-02, 最終更新日: 2024-06-19)

主引用文献

Raulinaitis, V.,Tossavainen, H.,Aitio, O.,Juuti, J.T.,Hiramatsu, K.,Kontinen, V.,Permi, P.
Identification and structural characterization of LytU, a unique peptidoglycan endopeptidase from the lysostaphin family.
Sci Rep, 7:6020-6020, 2017

PubMed Abstract: We introduce LytU, a short member of the lysostaphin family of zinc-dependent pentaglycine endopeptidases. It is a potential antimicrobial agent for S. aureus infections and its gene transcription is highly upregulated upon antibiotic treatments along with other genes involved in cell wall synthesis. We found this enzyme to be responsible for the opening of the cell wall peptidoglycan layer during cell divisions in S. aureus. LytU is anchored in the plasma membrane with the active part residing in the periplasmic space. It has a unique Ile/Lys insertion at position 151 that resides in the catalytic site-neighbouring loop and is vital for the enzymatic activity but not affecting the overall structure common to the lysostaphin family. Purified LytU lyses S. aureus cells and cleaves pentaglycine, a reaction conveniently monitored by NMR spectroscopy. Substituting the cofactor zinc ion with a copper or cobalt ion remarkably increases the rate of pentaglycine cleavage. NMR and isothermal titration calorimetry further reveal that, uniquely for its family, LytU is able to bind a second zinc ion which is coordinated by catalytic histidines and is therefore inhibitory. The pH-dependence and high affinity of binding carry further physiological implications.

PubMed: 28729697
DOI: 10.1038/s41598-017-06135-w

実験手法

SOLUTION NMR