5I8L

Crystal structure of the full-length cell wall-binding module of Cpl7 mutant R223A

5I8L の概要

• エントリーDOI: 10.2210/pdb5i8l/pdb
• 分子名称: Lysozyme, GLYCEROL (3 entities in total)
• 機能のキーワード: cell-wall binding domain, hydrolase
• 由来する生物種: Streptococcus phage Cp-7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15709.95

構造登録者

Bernardo-Garcia, N.,Silva-Martin, N.,Uson, I.,Hermoso, J.A. (登録日: 2016-02-19, 公開日: 2017-03-08, 最終更新日: 2024-01-10)

主引用文献

Bustamante, N.,Iglesias-Bexiga, M.,Bernardo-Garcia, N.,Silva-Martin, N.,Garcia, G.,Campanero-Rhodes, M.A.,Garcia, E.,Uson, I.,Buey, R.M.,Garcia, P.,Hermoso, J.A.,Bruix, M.,Menendez, M.
Deciphering how Cpl-7 cell wall-binding repeats recognize the bacterial peptidoglycan.
Sci Rep, 7:16494-16494, 2017

PubMed Abstract: Endolysins, the cell wall lytic enzymes encoded by bacteriophages to release the phage progeny, are among the top alternatives to fight against multiresistant pathogenic bacteria; one of the current biggest challenges to global health. Their narrow range of susceptible bacteria relies, primarily, on targeting specific cell-wall receptors through specialized modules. The cell wall-binding domain of Cpl-7 endolysin, made of three CW_7 repeats, accounts for its extended-range of substrates. Using as model system the cell wall-binding domain of Cpl-7, here we describe the molecular basis for the bacterial cell wall recognition by the CW_7 motif, which is widely represented in sequences of cell wall hydrolases. We report the crystal and solution structure of the full-length domain, identify N-acetyl-D-glucosaminyl-(β1,4)-N-acetylmuramyl-L-alanyl-D-isoglutamine (GMDP) as the peptidoglycan (PG) target recognized by the CW_7 motifs, and characterize feasible GMDP-CW_7 contacts. Our data suggest that Cpl-7 cell wall-binding domain might simultaneously bind to three PG chains, and also highlight the potential use of CW_7-containing lysins as novel anti-infectives.

PubMed: 29184076
DOI: 10.1038/s41598-017-16392-4

実験手法

X-RAY DIFFRACTION (2.801 Å)