2gr8: Difference between revisions

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 ==Hia 1022-1098==
-<StructureSection load='2gr8' size='340' side='right' caption='[[2gr8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='2gr8' size='340' side='right'caption='[[2gr8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2gr8]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GR8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GR8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2gr8]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GR8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GR8 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gr7|2gr7]]</td></tr>
+</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&#8491;</td></tr>
-<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=2gr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gr8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2gr8 RCSB], [http://www.ebi.ac.uk/pdbsum/2gr8 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=2gr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gr8 OCA], [https://pdbe.org/2gr8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gr8 RCSB], [https://www.ebi.ac.uk/pdbsum/2gr8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gr8 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q48152_HAEIF Q48152_HAEIF]
 == 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/gr/2gr8_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gr/2gr8_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=2gr8 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Autotransporter proteins are defined by the ability to drive their own secretion across the bacterial outer membrane. The Hia autotransporter of Haemophilus influenzae belongs to the trimeric autotransporter subfamily and mediates bacterial adhesion to the respiratory epithelium. In this report, we present the crystal structure of the C-terminal end of Hia, corresponding to the entire Hia translocator domain and part of the passenger domain (residues 992-1098). This domain forms a beta-barrel with 12 transmembrane beta-strands, including four strands from each subunit. The beta-barrel has a central channel of 1.8 nm in diameter that is traversed by three N-terminal alpha-helices, one from each subunit. Mutagenesis studies demonstrate that the transmembrane portion of the three alpha-helices and the loop region between the alpha-helices and the neighboring beta-strands are essential for stability of the trimeric structure of the translocator domain, and that trimerization of the translocator domain is a prerequisite for translocator activity. Overall, this study provides important insights into the mechanism of translocation in trimeric autotransporters.
-Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter.,Meng G, Surana NK, St Geme JW 3rd, Waksman G EMBO J. 2006 Jun 7;25(11):2297-304. Epub 2006 May 11. PMID:16688217<ref>PMID:16688217</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+==See Also==
-</div>
+*[[Adhesin 3D structures|Adhesin 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Haemophilus influenzae]]
-[[Category: Meng, G]]
+[[Category: Large Structures]]
-[[Category: Waksman, G]]
+[[Category: Meng G]]
-[[Category: Adhesion]]
+[[Category: Waksman G]]
-[[Category: Membrane protein]]
-[[Category: Microbial pathogenesis]]
-[[Category: Protein secretion]]
-[[Category: Trimeric autotransporter]]