2vq2: Difference between revisions
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< | ==Crystal structure of PilW, widely conserved type IV pilus biogenesis factor== | ||
<StructureSection load='2vq2' size='340' side='right'caption='[[2vq2]], [[Resolution|resolution]] 1.54Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2vq2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VQ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VQ2 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]] 1.54Å</td></tr> | |||
--> | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO3:SULFITE+ION'>SO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2vq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vq2 OCA], [https://pdbe.org/2vq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vq2 RCSB], [https://www.ebi.ac.uk/pdbsum/2vq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vq2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9JZ41_NEIMB Q9JZ41_NEIMB] | |||
== 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/vq/2vq2_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2vq2 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Type IV pili (Tfp) are arguably the most widespread pili in bacteria, whose biogenesis requires a complex machinery composed of as many as 18 different proteins. This includes the conserved outer membrane-localized secretin, which forms a pore through which Tfp emerge on the bacterial surface. Although, in most model species studied, secretin oligomerization and functionality requires the action of partner lipoproteins, structural information regarding these molecules is limited. We report the high-resolution crystal structure of PilW, the partner lipoprotein of the type IV pilus secretin PilQ from Neisseria meningitidis, which defines a conserved class of Tfp biogenesis proteins involved in the formation and/or stability of secretin multimers in a wide variety of bacteria. The use of the PilW structure as a blueprint reveals an area of high-level sequence conservation in homologous proteins from different pathogens that could reflect a possible secretin-binding site. These results could be exploited for the development of new broad-spectrum antibacterials interfering with the biogenesis of a widespread virulence factor. | Type IV pili (Tfp) are arguably the most widespread pili in bacteria, whose biogenesis requires a complex machinery composed of as many as 18 different proteins. This includes the conserved outer membrane-localized secretin, which forms a pore through which Tfp emerge on the bacterial surface. Although, in most model species studied, secretin oligomerization and functionality requires the action of partner lipoproteins, structural information regarding these molecules is limited. We report the high-resolution crystal structure of PilW, the partner lipoprotein of the type IV pilus secretin PilQ from Neisseria meningitidis, which defines a conserved class of Tfp biogenesis proteins involved in the formation and/or stability of secretin multimers in a wide variety of bacteria. The use of the PilW structure as a blueprint reveals an area of high-level sequence conservation in homologous proteins from different pathogens that could reflect a possible secretin-binding site. These results could be exploited for the development of new broad-spectrum antibacterials interfering with the biogenesis of a widespread virulence factor. | ||
Structure of a widely conserved type IV pilus biogenesis factor that affects the stability of secretin multimers.,Trindade MB, Job V, Contreras-Martel C, Pelicic V, Dessen A J Mol Biol. 2008 May 16;378(5):1031-9. Epub 2008 Mar 19. PMID:18433773<ref>PMID:18433773</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2vq2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Neisseria meningitidis]] | [[Category: Neisseria meningitidis]] | ||
[[Category: Contreras-Martel C]] | |||
[[Category: Contreras-Martel | [[Category: Dessen A]] | ||
[[Category: Dessen | [[Category: Job V]] | ||
[[Category: Job | [[Category: Pelicic V]] | ||
[[Category: Pelicic | [[Category: Trinidade MB]] | ||
[[Category: Trinidade | |||
