3vjr

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==Crystal structure of Peptidyl-tRNA hydrolase from Escherichia coli in complex with the CCA-acceptor-T[PSI]C domain of tRNA==
==Crystal structure of Peptidyl-tRNA hydrolase from Escherichia coli in complex with the CCA-acceptor-T[PSI]C domain of tRNA==
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<StructureSection load='3vjr' size='340' side='right' caption='[[3vjr]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='3vjr' size='340' side='right'caption='[[3vjr]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3vjr]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VJR FirstGlance]. <br>
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<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>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pth, b1204, JW1195 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr>
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</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>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aminoacyl-tRNA_hydrolase Aminoacyl-tRNA hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.29 3.1.1.29] </span></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vjr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vjr RCSB], [http://www.ebi.ac.uk/pdbsum/3vjr PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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.
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[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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 3vjr" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aminoacyl-tRNA hydrolase]]
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[[Category: Escherichia coli K-12]]
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[[Category: Escherichia coli k-12]]
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[[Category: Large Structures]]
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[[Category: Ito, K]]
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[[Category: Ito K]]
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[[Category: Miura, K I]]
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[[Category: Miura KI]]
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[[Category: Mochizuki, M]]
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[[Category: Mochizuki M]]
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[[Category: Murakami, R]]
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[[Category: Murakami R]]
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[[Category: Qi, H]]
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[[Category: Qi H]]
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[[Category: Shimizu, Y]]
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[[Category: Shimizu Y]]
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[[Category: Uchiumi, T]]
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[[Category: Uchiumi T]]
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[[Category: Ueda, T]]
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[[Category: Ueda T]]
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[[Category: Hydrolase-rna complex]]
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[[Category: Peptidyl-trna hydrolase]]
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[[Category: Seven beta-strands form]]
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Current revision

Crystal structure of Peptidyl-tRNA hydrolase from Escherichia coli in complex with the CCA-acceptor-T[PSI]C domain of tRNA

PDB ID 3vjr

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