2L97

Solution structure of HtrA PDZ domain from Streptococcus pneumoniae

Summary for 2L97

• Entry DOI: 10.2210/pdb2l97/pdb
• NMR Information: BMRB: 16653
• Descriptor: Putative serine protease (1 entity in total)
• Functional Keywords: htra-pdz, protein binding
• Biological source: Streptococcus pneumoniae
• Total number of polymer chains: 1
• Total formula weight: 14890.76

Authors

Fan, K.,Zhang, J.,Zhang, X.,Tu, X. (deposition date: 2011-02-02, release date: 2012-01-18, Last modification date: 2024-05-15)

Primary citation

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

Experimental method

SOLUTION NMR