4FET

Catalytic domain of germination-specific lytic tansglycosylase SleB from Bacillus anthracis

4FET の概要

• エントリーDOI: 10.2210/pdb4fet/pdb
• 分子名称: Spore cortex-lytic enzyme prepeptide, SODIUM ION (3 entities in total)
• 機能のキーワード: transglycosylase, cortex hydrolase domain, sodium ion, semet, cortex, hydrolase
• 由来する生物種: Bacillus anthracis (anthrax,anthrax bacterium)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48787.80

構造登録者

Jing, X.,Heffron, J.,Popham, D.L.,Schubot, F.D. (登録日: 2012-05-30, 公開日: 2012-07-25, 最終更新日: 2024-10-30)

主引用文献

Jing, X.,Robinson, H.R.,Heffron, J.D.,Popham, D.L.,Schubot, F.D.
The catalytic domain of the germination-specific lytic transglycosylase SleB from Bacillus anthracis displays a unique active site topology.
Proteins, 80:2469-2475, 2012

PubMed Abstract: Bacillus anthracis produces metabolically inactive spores. Germination of these spores requires germination-specific lytic enzymes (GSLEs) that degrade the unique cortex peptidoglycan to permit resumption of metabolic activity and outgrowth. We report the first crystal structure of the catalytic domain of a GSLE, SleB. The structure revealed a transglycosylase fold with unique active site topology and permitted identification of the catalytic glutamate residue. Moreover, the structure provided insights into the molecular basis for the specificity of the enzyme for muramic-δ-lactam-containing cortex peptidoglycan. The protein also contains a metal-binding site that is positioned directly at the entrance of the substrate-binding cleft.

PubMed: 22777830
DOI: 10.1002/prot.24140

実験手法

X-RAY DIFFRACTION (1.909 Å)