2L97

Solution structure of HtrA PDZ domain from Streptococcus pneumoniae

2L97 の概要

• エントリーDOI: 10.2210/pdb2l97/pdb
• NMR情報: BMRB: 16653
• 分子名称: Putative serine protease (1 entity in total)
• 機能のキーワード: htra-pdz, protein binding
• 由来する生物種: Streptococcus pneumoniae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14890.76

構造登録者

Fan, K.,Zhang, J.,Zhang, X.,Tu, X. (登録日: 2011-02-02, 公開日: 2012-01-18, 最終更新日: 2024-05-15)

主引用文献

Fan, K.,Zhang, J.,Zhang, X.,Tu, X.
Solution structure of HtrA PDZ domain from Streptococcus pneumoniae and its interaction with YYF-COOH containing peptides.
J.Struct.Biol., 176:16-23, 2011

PubMed Abstract: High-temperature requirement A (HtrA), a highly conserved family of serine protease, plays crucial roles in protein quality control in prokaryotes and eukaryotes. The HtrA protein contains a C-terminal PDZ domain that mediates the proteolytic activity. Here we reported the solution structure of the HtrA PDZ domain from Streptococcus pneumoniae by NMR spectroscopy. Our results showed that the structure of HtrA PDZ domain, which contains three α-helices and five β-strands, illustrates conservation within the canonical PDZ domains. In addition, we demonstrated the interactions between S. pneumoniae HtrA PDZ domain and peptides with the motif XXX-YYF-COOH by surface plasmon resonance. Besides, we identified the ligand binding surface and the critical residues responsible for ligand binding of HtrA PDZ domain by chemical shift perturbation and site-directed mutagenesis.

PubMed: 21757011
DOI: 10.1016/j.jsb.2011.06.009

実験手法

SOLUTION NMR