2obl
From Proteopedia
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| - | [[Image:2obl.gif|left|200px]] | ||
| - | < | + | ==Structural and biochemical analysis of a prototypical ATPase from the type III secretion system of pathogenic bacteria== |
| - | + | <StructureSection load='2obl' size='340' side='right'caption='[[2obl]], [[Resolution|resolution]] 1.80Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2obl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O127:H6_str._E2348/69 Escherichia coli O127:H6 str. E2348/69]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OBL FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | |
| - | --> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></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=2obl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2obl OCA], [https://pdbe.org/2obl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2obl RCSB], [https://www.ebi.ac.uk/pdbsum/2obl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2obl ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/B7UMA6_ECO27 B7UMA6_ECO27] | |
| - | + | == 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/ob/2obl_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/main_output.php?pdb_ID=2obl ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The type III secretion system (T3SS) ATPase is the conserved and essential inner-membrane component involved in the initial stages of selective secretion of specialized T3SS virulence effector proteins from the bacterial cytoplasm through to the infected host cell, a process crucial to subsequent pathogenicity. Here we present the 1.8-A-resolution crystal structure of the catalytic domain of the prototypical T3SS ATPase EscN from enteropathogenic Escherichia coli (EPEC). Along with in vitro and in vivo mutational analysis, our data show that the T3SS ATPases share similarity with the F1 ATPases but have important structural and sequence differences that dictate their unique secretory role. We also show that T3SS ATPase activity is dependent on EscN oligomerization and describe the molecular features and possible functional implications of a hexameric ring model. | The type III secretion system (T3SS) ATPase is the conserved and essential inner-membrane component involved in the initial stages of selective secretion of specialized T3SS virulence effector proteins from the bacterial cytoplasm through to the infected host cell, a process crucial to subsequent pathogenicity. Here we present the 1.8-A-resolution crystal structure of the catalytic domain of the prototypical T3SS ATPase EscN from enteropathogenic Escherichia coli (EPEC). Along with in vitro and in vivo mutational analysis, our data show that the T3SS ATPases share similarity with the F1 ATPases but have important structural and sequence differences that dictate their unique secretory role. We also show that T3SS ATPase activity is dependent on EscN oligomerization and describe the molecular features and possible functional implications of a hexameric ring model. | ||
| - | + | Structural analysis of a prototypical ATPase from the type III secretion system.,Zarivach R, Vuckovic M, Deng W, Finlay BB, Strynadka NC Nat Struct Mol Biol. 2007 Feb;14(2):131-7. Epub 2007 Jan 21. PMID:17237797<ref>PMID:17237797</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: Escherichia coli]] | + | <div class="pdbe-citations 2obl" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Deng | + | <references/> |
| - | [[Category: Finlay | + | __TOC__ |
| - | [[Category: Strynadka | + | </StructureSection> |
| - | [[Category: Vuckovic | + | [[Category: Escherichia coli O127:H6 str. E2348/69]] |
| - | [[Category: Zarivach | + | [[Category: Large Structures]] |
| - | + | [[Category: Deng W]] | |
| - | + | [[Category: Finlay BB]] | |
| + | [[Category: Strynadka NCJ]] | ||
| + | [[Category: Vuckovic M]] | ||
| + | [[Category: Zarivach R]] | ||
Current revision
Structural and biochemical analysis of a prototypical ATPase from the type III secretion system of pathogenic bacteria
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