3HC7

Crystal structure of lysin B from Mycobacteriophage D29

3HC7 の概要

• エントリーDOI: 10.2210/pdb3hc7/pdb
• 分子名称: Gene 12 protein (2 entities in total)
• 機能のキーワード: alpha/beta sandwich, cell adhesion
• 由来する生物種: Mycobacterium phage D29
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28546.68

構造登録者

Sun, Q.,Sacchettini, J.C. (登録日: 2009-05-05, 公開日: 2009-07-21, 最終更新日: 2024-02-21)

主引用文献

Payne, K.,Sun, Q.,Sacchettini, J.,Hatfull, G.F.
Mycobacteriophage Lysin B is a novel mycolylarabinogalactan esterase
Mol.Microbiol., 73:367-381, 2009

PubMed Abstract: Mycobacteriophages encounter a unique problem among phages of Gram-positive bacteria, in that lysis must not only degrade the peptidoglycan layer but also circumvent a mycolic acid-rich outer membrane covalently attached to the arabinogalactan-peptidoglycan complex. Mycobacteriophages accomplish this by producing two lysis enzymes, Lysin A (LysA) that hydrolyses peptidoglycan, and Lysin B (LysB), a novel mycolylarabinogalactan esterase, that cleaves the mycolylarabinogalactan bond to release free mycolic acids. The D29 LysB structure shows an alpha/beta hydrolase organization with a catalytic triad common to cutinases, but which contains an additional four-helix domain implicated in the binding of lipid substrates. Whereas LysA is essential for mycobacterial lysis, a Giles DeltalysB mutant mycobacteriophage is viable, but defective in the normal timing, progression and completion of host cell lysis. We propose that LysB facilitates lysis by compromising the integrity of the mycobacterial outer membrane linkage to the arabinogalactan-peptidoglycan layer.

PubMed: 19555454
DOI: 10.1111/j.1365-2958.2009.06775.x

実験手法

X-RAY DIFFRACTION (2 Å)