4X36

Crystal structure of the autolysin LytA from Streptococcus pneumoniae TIGR4

4X36 の概要

• エントリーDOI: 10.2210/pdb4x36/pdb
• 分子名称: Autolysin, GLYCEROL, ZINC ION, ... (5 entities in total)
• 機能のキーワード: autolysin, amidase, hydrolase
• 由来する生物種: Streptococcus pneumoniae TIGR4
• 細胞内の位置: Secreted : P06653
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38053.35

構造登録者

Cheng, W.,Li, Q.,Zhou, C.Z.,Chen, Y.X. (登録日: 2014-11-28, 公開日: 2015-05-27, 最終更新日: 2024-10-30)

主引用文献

Li, Q.,Cheng, W.,Morlot, C.,Bai, X.H.,Jiang, Y.L.,Wang, W.,Roper, D.I.,Vernet, T.,Dong, Y.H.,Chen, Y.,Zhou, C.Z.
Full-length structure of the major autolysin LytA.
Acta Crystallogr.,Sect.D, 71:1373-1381, 2015

PubMed Abstract: LytA is responsible for the autolysis of many Streptococcus species, including pathogens such as S. pneumoniae, S. pseudopneumoniae and S. mitis. However, how this major autolysin achieves full activity remains unknown. Here, the full-length structure of the S. pneumoniae LytA dimer is reported at 2.1 Å resolution. Each subunit has an N-terminal amidase domain and a C-terminal choline-binding domain consisting of six choline-binding repeats, which form five canonical and one single-layered choline-binding sites. Site-directed mutageneses combined with enzymatic activity assays indicate that dimerization and binding to choline are two independent requirements for the autolytic activity of LytA in vivo. Altogether, it is suggested that dimerization and full occupancy of all choline-binding sites through binding to choline-containing TA chains enable LytA to adopt a fully active conformation which allows the amidase domain to cleave two lactyl-amide bonds located about 103 Å apart on the peptidoglycan.

PubMed: 26057677
DOI: 10.1107/S1399004715007403

実験手法

X-RAY DIFFRACTION (2.101 Å)