2gqc: Difference between revisions

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 ==Solution structure of the N-terminal domain of Rhomboid Intramembrane Protease from P. aeruginosa==
-<StructureSection load='2gqc' size='340' side='right' caption='[[2gqc]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2gqc' size='340' side='right'caption='[[2gqc]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2gqc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GQC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GQC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2gqc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GQC FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Rhomboid_protease Rhomboid protease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.105 3.4.21.105] </span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gqc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2gqc RCSB], [http://www.ebi.ac.uk/pdbsum/2gqc PDBsum]</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=2gqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gqc OCA], [https://pdbe.org/2gqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gqc RCSB], [https://www.ebi.ac.uk/pdbsum/2gqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gqc ProSAT]</span></td></tr>
-<table>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9HZC2_PSEAE Q9HZC2_PSEAE]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gq/2gqc_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gq/2gqc_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
-</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/chain_selection.php?pdb_ID=2ata 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=2gqc ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Rhomboids are ubiquitous integral membrane proteases that release cellular signals from membrane-bound substrates through a general signal transduction mechanism known as regulated intramembrane proteolysis (RIP). We present the NMR structure of the cytosolic N-terminal domain (NRho) of P. aeruginosa Rhomboid. NRho consists of a novel alpha/beta fold and represents the first detailed structural insight into this class of intramembrane proteases. We find evidence that NRho is capable of strong and specific association with detergent micelles that mimic the membrane/water interface. Relaxation measurements on NRho reveal structural fluctuations on the microseconds-milliseconds timescale in regions including and contiguous to those implicated in membrane interaction. This structural plasticity may facilitate the ability of NRho to recognize and associate with membranes. We suggest that NRho plays a role in scissile peptide bond selectivity by optimally positioning the Rhomboid active site relative to the membrane plane.
-Solution structure and dynamics of the N-terminal cytosolic domain of rhomboid intramembrane protease from Pseudomonas aeruginosa: insights into a functional role in intramembrane proteolysis.,Del Rio A, Dutta K, Chavez J, Ubarretxena-Belandia I, Ghose R J Mol Biol. 2007 Jan 5;365(1):109-22. Epub 2006 Sep 23. PMID:17059825<ref>PMID:17059825</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
 ==See Also==
 *[[Rhomboid protease|Rhomboid protease]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Pseudomonas aeruginosa]]
+[[Category: Large Structures]]
-[[Category: Rhomboid protease]]
+[[Category: Pseudomonas aeruginosa PAO1]]
-[[Category: Chavez, J.]]
+[[Category: Chavez J]]
-[[Category: Dutta, K.]]
+[[Category: Del Rio A]]
-[[Category: Ghose, R.]]
+[[Category: Dutta K]]
-[[Category: Rio, A Del.]]
+[[Category: Ghose R]]
-[[Category: Ubarretxena-Belandia, I.]]
+[[Category: Ubarretxena-Belandia I]]
-[[Category: Alpha-beta domain]]
-[[Category: Hydrolase]]