2grm

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Current revision (09:29, 14 February 2024) (edit) (undo)
 
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<StructureSection load='2grm' size='340' side='right'caption='[[2grm]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='2grm' size='340' side='right'caption='[[2grm]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2grm]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/"enterococcus_proteiformis"_thiercelin_and_jouhaud_1903 "enterococcus proteiformis" thiercelin and jouhaud 1903]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GRM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GRM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2grm]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GRM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GRM FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2grl|2grl]]</div></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&#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=2grm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2grm OCA], [https://pdbe.org/2grm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2grm RCSB], [https://www.ebi.ac.uk/pdbsum/2grm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2grm ProSAT]</span></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=2grm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2grm OCA], [https://pdbe.org/2grm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2grm RCSB], [https://www.ebi.ac.uk/pdbsum/2grm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2grm ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q04114_ENTFL Q04114_ENTFL]
== 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=2grm 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=2grm 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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In many bacteria expression of lateral gene transfer and of virulence factors is controlled by cell-cell signalling systems. Molecular interactions of microbial signal molecules with their cognate receptors are not well understood. For the Enterococcus faecalis conjugative plasmid pCF10, the PrgX protein serves as a molecular switch controlling expression of conjugation and virulence genes encoded by the plasmid. The induction state of a pCF10-carrying donor cell is determined by the ratio of two signalling peptides, cCF10 pheromone and iCF10 inhibitor. Recent analysis of PrgX/cCF10 interactions suggests a mechanism for conversion to the induced state. However, the means by which iCF10 peptide antagonizes cCF10 activity is unclear, and it has been suggested that inhibitor peptides block import of pheromone peptides. We now show that both of these peptides interact with the same binding pocket of PrgX, but they differentially alter the conformation of the protein and its oligomerization state, resulting in opposing biological activities.
 
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Molecular basis for control of conjugation by bacterial pheromone and inhibitor peptides.,Kozlowicz BK, Shi K, Gu ZY, Ohlendorf DH, Earhart CA, Dunny GM Mol Microbiol. 2006 Nov;62(4):958-69. Epub 2006 Oct 13. PMID:17038121<ref>PMID:17038121</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 2grm" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Enterococcus proteiformis thiercelin and jouhaud 1903]]
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[[Category: Enterococcus faecalis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Dunny, G M]]
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[[Category: Dunny GM]]
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[[Category: Earhart, C A]]
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[[Category: Earhart CA]]
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[[Category: Gu, Z Y]]
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[[Category: Gu ZY]]
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[[Category: Kozlowicz, B K]]
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[[Category: Kozlowicz BK]]
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[[Category: Ohlendorf, D H]]
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[[Category: Ohlendorf DH]]
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[[Category: Shi, K]]
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[[Category: Shi K]]
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[[Category: Inhibitor]]
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[[Category: Receptor]]
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[[Category: Transcription]]
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Current revision

Crystal structure of PrgX/iCF10 complex

PDB ID 2grm

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