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 | |
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 Cited by 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: 21757011DOI: 10.1016/j.jsb.2011.06.009 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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