Structural highlights
Function
Q885L4_PSESM
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The NMR structure of the peptidyl-tRNA hydrolase (PTH) domain from Pseudomonas syringae (P. syringae PTH domain) was solved by using recently devised protocol for high throughput protein structure determination. The P. syringae PTH domain belongs to a large Pfam family PF00472, which consists of at least 1549 proteins annotated as 'hydrolysis domains of peptidyl-tRNA'. The structure of P. syringae PTH domain expands the 'structural coverage' of the PFam family.
NMR structure of the peptidyl-tRNA hydrolase domain from Pseudomonas syringae expands the structural coverage of the hydrolysis domains of class 1 peptide chain release factors.,Singarapu KK, Xiao R, Acton T, Rost B, Montelione GT, Szyperski T Proteins. 2008 May 1;71(2):1027-31. doi: 10.1002/prot.21947. PMID:18247350[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Singarapu KK, Xiao R, Acton T, Rost B, Montelione GT, Szyperski T. NMR structure of the peptidyl-tRNA hydrolase domain from Pseudomonas syringae expands the structural coverage of the hydrolysis domains of class 1 peptide chain release factors. Proteins. 2008 May 1;71(2):1027-31. PMID:18247350 doi:10.1002/prot.21947
