2o7l: Difference between revisions

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-{{Seed}}
+==The open-cap conformation of GlpG==
-[[Image:2o7l.png|left|200px]]
+<StructureSection load='2o7l' size='340' side='right' caption='[[2o7l]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2o7l]] is a 1 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=2O7L OCA]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene><br>
+<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ic8|2ic8]]</td></tr>
+<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glpG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
+<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></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=2o7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2o7l RCSB], [http://www.ebi.ac.uk/pdbsum/2o7l PDBsum]</span></td></tr>
+<table>
+== 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/o7/2o7l_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].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The active sites of intramembrane proteases are positioned in the lipid bilayer to facilitate peptide bond hydrolysis in the membrane. Previous crystallographic analysis of Escherichia coli GlpG, an intramembrane protease of the rhomboid family, has revealed an internal and hydrophilic active site in an apparently closed conformation. Here we describe the crystal structure of GlpG in a more open conformation, where the capping loop L5 has been lifted, exposing the previously buried and catalytically essential Ser-201 to outside aqueous solution. A water molecule now moves into the putative oxyanion hole that is constituted of a main-chain amide (Ser-201) and two conserved side chains (His-150 and Asn-154). The loop movement also destabilizes a hydrophobic side chain (Phe-245) previously buried between transmembrane helices S2 and S5 and creates a side portal from the lipid to protease active site. These results provide insights into the conformational plasticity of GlpG to accommodate substrate binding and catalysis and into the chirality of the reaction intermediate.
-<!--
+Open-cap conformation of intramembrane protease GlpG.,Wang Y, Ha Y Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2098-102. Epub 2007 Feb 2. PMID:17277078<ref>PMID:17277078</ref>
-The line below this paragraph, containing "STRUCTURE_2o7l", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
-{{STRUCTURE_2o7l|  PDB=2o7l  |  SCENE=  }}
-===The open-cap conformation of GlpG===
+From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+</div>
+== References ==
-<!--
+<references/>
-The line below this paragraph, {{ABSTRACT_PUBMED_17277078}}, adds the Publication Abstract to the page
+__TOC__
-(as it appears on PubMed at http://www.pubmed.gov), where 17277078 is the PubMed ID number.
+</StructureSection>
--->
+[[Category: Bacillus coli migula 1895]]
-{{ABSTRACT_PUBMED_17277078}}
-==About this Structure==
-O7L is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O7L OCA].
-==Reference==
-<ref group="xtra">PMID:17277078</ref><references group="xtra"/>
-[[Category: Escherichia coli]]
 [[Category: Ha, Y.]]
 [[Category: Glpg]]
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 [[Category: Membrane protein]]
 [[Category: Rhomboid protease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 21:33:28 2009''