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==Crystal Structure of Bordetella pertussis BvgS periplasmic VFT2 domain==
==Crystal Structure of Bordetella pertussis BvgS periplasmic VFT2 domain==
<StructureSection load='3mpk' size='340' side='right' caption='[[3mpk]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
<StructureSection load='3mpk' size='340' side='right'caption='[[3mpk]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3mpk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Borpe Borpe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MPK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MPK FirstGlance]. <br>
<table><tr><td colspan='2'>[[3mpk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bordetella_pertussis_Tohama_I Bordetella pertussis Tohama I]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MPK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MPK FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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]] 2.04&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mpl|3mpl]]</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=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BP1877, bvgS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=257313 BORPE])</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=3mpk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mpk OCA], [https://pdbe.org/3mpk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mpk RCSB], [https://www.ebi.ac.uk/pdbsum/3mpk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mpk ProSAT]</span></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=3mpk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mpk OCA], [http://pdbe.org/3mpk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mpk RCSB], [http://www.ebi.ac.uk/pdbsum/3mpk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mpk ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/BVGS_BORPE BVGS_BORPE]] Member of the two-component regulatory system BvgS/BvgA. Phosphorylates BvgA via a four-step phosphorelay in response to environmental signals.  
[https://www.uniprot.org/uniprot/BVGS_BORPE BVGS_BORPE] Member of the two-component regulatory system BvgS/BvgA. Phosphorylates BvgA via a four-step phosphorelay in response to environmental signals.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mp/3mpk_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mp/3mpk_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 21: Line 20:
</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=3mpk 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=3mpk ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Two-component sensory transduction systems control important bacterial programs. In Bordetella pertussis, expression of the virulence regulon is controlled by the unorthodox BvgAS two-component system. BvgS is the prototype of a family of sensor-kinases that harbor periplasmic domains homologous to bacterial solute-binding proteins. Although BvgAS is active under laboratory conditions, no activating signal has been identified, only negative modulators. Here we show that the second periplasmic domain of BvgS interacts with modulators and adopts a Venus flytrap (VFT) fold. X-ray crystallography reveals that the two lobes of VFT2 delimitate a ligand-binding cavity enclosing fortuitous ligands. Most substitutions of putative ligand-binding residues in the VFT2 cavity keep BvgS active, and alteration of the cavity's electrostatic potential affects responsiveness to modulation. The crystal structure of this VFT2 variant conferring constitutive kinase activity to BvgS shows a closed cavity with another nonspecific ligand. Thus, VFT2 is closed and active without a specific agonist ligand, in contrast to typical VFTs. Modulators are antagonists of VFT2 that interrupt signaling. BvgAS is active for most of the B. pertussis infectious cycle, consistent with the proposed mechanism.
Periplasmic domain of the sensor-kinase BvgS reveals a new paradigm for the Venus flytrap mechanism.,Herrou J, Bompard C, Wintjens R, Dupre E, Willery E, Villeret V, Locht C, Antoine R, Jacob-Dubuisson F Proc Natl Acad Sci U S A. 2010 Sep 20. PMID:20855615<ref>PMID:20855615</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3mpk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Borpe]]
[[Category: Bordetella pertussis Tohama I]]
[[Category: Antoine, R]]
[[Category: Large Structures]]
[[Category: Bompard, C]]
[[Category: Antoine R]]
[[Category: Dupre, E]]
[[Category: Bompard C]]
[[Category: Herrou, J]]
[[Category: Dupre E]]
[[Category: Jacob-Dubuisson, F]]
[[Category: Herrou J]]
[[Category: Locht, C]]
[[Category: Jacob-Dubuisson F]]
[[Category: Villeret, V]]
[[Category: Locht C]]
[[Category: Willery, E]]
[[Category: Villeret V]]
[[Category: Wintjens, R]]
[[Category: Willery E]]
[[Category: Sensor domain]]
[[Category: Wintjens R]]
[[Category: Signaling protein]]
[[Category: Venus flytrap]]

Latest revision as of 13:26, 21 February 2024

Crystal Structure of Bordetella pertussis BvgS periplasmic VFT2 domainCrystal Structure of Bordetella pertussis BvgS periplasmic VFT2 domain

Structural highlights

3mpk is a 1 chain structure with sequence from Bordetella pertussis Tohama I. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.04Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BVGS_BORPE Member of the two-component regulatory system BvgS/BvgA. Phosphorylates BvgA via a four-step phosphorelay in response to environmental signals.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

3mpk, resolution 2.04Å

Drag the structure with the mouse to rotate

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OCA
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