2JVA

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

Summary for 2JVA

• Entry DOI: 10.2210/pdb2jva/pdb
• NMR Information: BMRB: 15471
• Descriptor: Peptidyl-tRNA hydrolase domain protein (1 entity in total)
• Functional Keywords: gft nmr, hydrolase, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, nesg
• Biological source: Pseudomonas syringae pv. tomato
• Total number of polymer chains: 1
• Total formula weight: 12097.71

Authors

Singarapu, K.K.,Sukumaran, D.,Parish, D.,Eletsky, A.,Zhang, Q.,Zhao, L.,Jiang, M.,Maglaqui, M.,Xiao, R.,Liu, J.,Baran, M.C.,Swapna, G.V.T.,Huang, Y.J.,Acton, T.B.,Rost, B.,Montelione, G.T.,Szyperski, T.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2007-09-14, release date: 2007-10-02, Last modification date: 2024-05-08)

Primary citation

Singarapu, K.K.,Xiao, R.,Acton, T.,Rost, B.,Montelione, G.T.,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, 71:1027-1031, 2008

PubMed Abstract: The NMR structure of the peptidyl-tRNA hydrolase (PTH) domain from ( PTH domain) was solved by using recently devised protocol for high throughput protein structure determination. The 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 PTH domain expands the ‘structural coverage’ of the PFam family.

PubMed: 18247350
DOI: 10.1002/prot.21947

Experimental method

SOLUTION NMR