2jva

NMR solution structure of peptidyl-tRNA hydrolase domain protein from Pseudomonas syringae pv. tomato. Northeast Structural Genomics Consortium target PsR211

spinqualitylabelsall models 2jva Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2jva is a 1 chain structure with sequence from Pseudomonas syringae pv. tomato str. DC3000. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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