2b3t

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==Structure of complex between E. coli translation termination factor RF1 and the PrmC methyltransferase==
==Structure of complex between E. coli translation termination factor RF1 and the PrmC methyltransferase==
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<StructureSection load='2b3t' size='340' side='right' caption='[[2b3t]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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<StructureSection load='2b3t' size='340' side='right'caption='[[2b3t]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2b3t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B3T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2B3T FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2b3t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B3T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B3T FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></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]] 3.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ml5|1ml5]], [[1gqe|1gqe]], [[1nv8|1nv8]], [[1t43|1t43]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hemK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), prfA, sueB, uar ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=2b3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b3t OCA], [https://pdbe.org/2b3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b3t RCSB], [https://www.ebi.ac.uk/pdbsum/2b3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b3t 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=2b3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b3t OCA], [http://pdbe.org/2b3t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2b3t RCSB], [http://www.ebi.ac.uk/pdbsum/2b3t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2b3t ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PRMC_ECOLI PRMC_ECOLI]] Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif, i.e. on 'Gln-235' in RF1 and on 'Gln-252' in RF2.<ref>PMID:11805295</ref> <ref>PMID:11847124</ref> <ref>PMID:16364916</ref> [[http://www.uniprot.org/uniprot/RF1_ECOLI RF1_ECOLI]] Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.[HAMAP-Rule:MF_00093]
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[https://www.uniprot.org/uniprot/PRMC_ECOLI PRMC_ECOLI] Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif, i.e. on 'Gln-235' in RF1 and on 'Gln-252' in RF2.<ref>PMID:11805295</ref> <ref>PMID:11847124</ref> <ref>PMID:16364916</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2b3t ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2b3t ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Class I release factors bind to ribosomes in response to stop codons and trigger peptidyl-tRNA hydrolysis at the P site. Prokaryotic and eukaryotic RFs share one motif: a GGQ tripeptide positioned in a loop at the end of a stem region that interacts with the ribosomal peptidyl transferase center. The glutamine side chain of this motif is specifically methylated in both prokaryotes and eukaryotes. Methylation in E. coli is due to PrmC and results in strong stimulation of peptide chain release. We have solved the crystal structure of the complex between E. coli RF1 and PrmC bound to the methyl donor product AdoHCy. Both the GGQ domain (domain 3) and the central region (domains 2 and 4) of RF1 interact with PrmC. Structural and mutagenic data indicate a compact conformation of RF1 that is unlike its conformation when it is bound to the ribosome but is similar to the crystal structure of the protein alone.
 
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Molecular basis for bacterial class I release factor methylation by PrmC.,Graille M, Heurgue-Hamard V, Champ S, Mora L, Scrima N, Ulryck N, van Tilbeurgh H, Buckingham RH Mol Cell. 2005 Dec 22;20(6):917-27. PMID:16364916<ref>PMID:16364916</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 2b3t" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus coli migula 1895]]
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[[Category: Escherichia coli]]
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[[Category: Buckingham, R H]]
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[[Category: Large Structures]]
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[[Category: Champ, S]]
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[[Category: Buckingham RH]]
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[[Category: Graille, M]]
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[[Category: Champ S]]
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[[Category: Heurgue-Hamard, V]]
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[[Category: Graille M]]
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[[Category: Mora, L]]
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[[Category: Heurgue-Hamard V]]
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[[Category: Scrima, N]]
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[[Category: Mora L]]
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[[Category: Tilbeurgh, H van]]
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[[Category: Scrima N]]
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[[Category: Ulryck, N]]
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[[Category: Ulryck N]]
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[[Category: Conformational change]]
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[[Category: Van Tilbeurgh H]]
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[[Category: Methylation]]
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[[Category: Release factor]]
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[[Category: Translation]]
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[[Category: Translation termination]]
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Current revision

Structure of complex between E. coli translation termination factor RF1 and the PrmC methyltransferase

PDB ID 2b3t

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