4S3J

Crystal structure of the Bacillus cereus spore cortex-lytic enzyme SleL

4S3J の概要

• エントリーDOI: 10.2210/pdb4s3j/pdb
• 関連するPDBエントリー: 3CZ8 4F55 4FET 4S3K
• 分子名称: Cortical-lytic enzyme, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: tim barrel, n-acetylglucosaminidase, spore cortex, hydrolase
• 由来する生物種: Bacillus cereus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 145776.63

構造登録者

Christie, G.,Chirgadze, D.Y.,Ustok, F.I. (登録日: 2015-02-04, 公開日: 2015-08-19, 最終更新日: 2023-09-20)

主引用文献

Ustok, F.I.,Chirgadze, D.Y.,Christie, G.
Structural and functional analysis of SleL, a peptidoglycan lysin involved in germination of Bacillus spores.
Proteins, 83:1787-1799, 2015

PubMed Abstract: A major event in the germination of Bacillus spores concerns hydrolysis of the cortical peptidoglycan that surrounds the spore protoplast, the integrity of which is essential for maintenance of dormancy. Cortex degradation is initiated in all species of Bacillus spores by the combined activity of two semi-redundant cortex-lytic enzymes, SleB and CwlJ. A third enzyme, SleL, which has N-acetylglucosaminidase activity, cleaves peptidoglycan fragments generated by SleB and CwlJ. Here we present crystal structures of B. cereus and B. megaterium SleL at 1.6 angstroms and 1.7 angstroms, respectively. The structures were determined with a view to identifying the structural basis of differences in catalytic efficiency between the respective enzymes. The catalytic (α/β)8 -barrel cores of both enzymes are highly conserved from a structural perspective, including the spatial distribution of the catalytic residues. Both enzymes are equipped with two N-terminal peptidoglycan-binding LysM domains, which are also structurally highly conserved. However, the topological arrangement of the respective enzymes second LysM domain is markedly different, and this may account for differences in catalytic rates by impacting upon the position of the active sites with respect to their substrates. A chimeric enzyme comprising the B. megaterium SleL catalytic domain plus B. cereus SleL LysM domains displayed enzymatic activity comparable to the native B. cereus protein, exemplifying the importance of the LysM domains to SleL function. Similarly, the reciprocal construct, comprising the B. cereus SleL catalytic domain with B. megaterium SleL LysM domains, showed reduced activity compared with native B. cereus SleL.

PubMed: 26190134
DOI: 10.1002/prot.24861

実験手法

X-RAY DIFFRACTION (1.6 Å)