Peptidyl-tRNA hydrolase
From Proteopedia
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<StructureSection load='3vjr' size='350' side='right' caption='Structure of peptidyl-tRNA hydrolase complex with tRNA CCA acceptor domain (PDB entry [[3vjr]])' scene=''> | <StructureSection load='3vjr' size='350' side='right' caption='Structure of peptidyl-tRNA hydrolase complex with tRNA CCA acceptor domain (PDB entry [[3vjr]])' scene=''> | ||
| + | == Function == | ||
| + | '''Peptidyl-tRNA hydrolase''' (PTH) is a bacterial enzyme which cleaves peptidyl-tRNA to free peptide and tRNA<ref>PMID:16849786</ref>. PTH catalyzes the reaction in cases of aborted translation for recycling the tRNA for further rounds of protein synthesis. PTH is essential for bacterial viability. | ||
| - | ' | + | == Structural highlights == |
| - | + | PTH dimer interacts with tRNA at the latter's CCA - the 3' end of the molecule which binds the amino acid; the acceptor site which pass-pairs tRNA N-terminal nucleotides to the C-terminal nucleotides and the TΨC site (Ψ is pseudouridine) which is the tRNA ribosome recognition site<ref>PMID:22923517</ref>. | |
</StructureSection> | </StructureSection> | ||
Revision as of 06:40, 21 June 2016
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3D Structures of peptidyl-tRNA hydrolase
Updated on 21-June-2016
References
- ↑ Das G, Varshney U. Peptidyl-tRNA hydrolase and its critical role in protein biosynthesis. Microbiology. 2006 Aug;152(Pt 8):2191-5. PMID:16849786 doi:http://dx.doi.org/10.1099/mic.0.29024-0
- ↑ Ito K, Murakami R, Mochizuki M, Qi H, Shimizu Y, Miura KI, Ueda T, Uchiumi T. Structural basis for the substrate recognition and catalysis of peptidyl-tRNA hydrolase. Nucleic Acids Res. 2012 Aug 25. PMID:22923517 doi:10.1093/nar/gks790
