View source for 3vjr


==Crystal structure of Peptidyl-tRNA hydrolase from Escherichia coli in complex with the CCA-acceptor-T[PSI]C domain of tRNA==
<StructureSection load='3vjr' size='340' side='right'caption='[[3vjr]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3vjr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VJR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vjr OCA], [https://pdbe.org/3vjr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vjr RCSB], [https://www.ebi.ac.uk/pdbsum/3vjr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vjr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PTH_ECOLI PTH_ECOLI] The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. Involved in lambda inhibition of host protein synthesis. PTH activity may, directly or indirectly, be the target for lambda bar RNA leading to rap cell death.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Peptidyl-tRNA hydrolase (Pth) cleaves the ester bond between the peptide and the tRNA of peptidyl-tRNA molecules, which are produced by aborted translation, to recycle tRNA for further rounds of protein synthesis. Pth is ubiquitous in nature, and its enzymatic activity is essential for bacterial viability. We have determined the crystal structure of Escherichia coli Pth in complex with the tRNA CCA-acceptor-TPsiC domain, the enzyme-binding region of the tRNA moiety of the substrate, at 2.4 A resolution. In combination with site-directed mutagenesis studies, the structure identified the amino acid residues involved in tRNA recognition. The structure also revealed that Pth interacts with the tRNA moiety through the backbone phosphates and riboses, and no base-specific interactions were observed, except for the interaction with the highly conserved base G53. This feature enables Pth to accept the diverse sequences of the elongator-tRNAs as substrate components. Furthermore, we propose an authentic Pth:peptidyl-tRNA complex model and a detailed mechanism for the hydrolysis reaction, based on the present crystal structure and the previous studies' results.

Structural basis for the substrate recognition and catalysis of peptidyl-tRNA hydrolase.,Ito K, Murakami R, Mochizuki M, Qi H, Shimizu Y, Miura KI, Ueda T, Uchiumi T Nucleic Acids Res. 2012 Aug 25. PMID:22923517<ref>PMID:22923517</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3vjr" style="background-color:#fffaf0;"></div>

==See Also==
*[[Peptidyl-tRNA hydrolase|Peptidyl-tRNA hydrolase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Ito K]]
[[Category: Miura KI]]
[[Category: Mochizuki M]]
[[Category: Murakami R]]
[[Category: Qi H]]
[[Category: Shimizu Y]]
[[Category: Uchiumi T]]
[[Category: Ueda T]]