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5bwj

From Proteopedia

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<StructureSection load='5bwj' size='340' side='right'caption='[[5bwj]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
<StructureSection load='5bwj' size='340' side='right'caption='[[5bwj]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5bwj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Borbu Borbu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BWJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BWJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5bwj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Borreliella_burgdorferi_B31 Borreliella burgdorferi B31]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BWJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BWJ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.054&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BB_0420 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224326 BORBU])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
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<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=5bwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bwj OCA], [http://pdbe.org/5bwj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bwj RCSB], [http://www.ebi.ac.uk/pdbsum/5bwj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bwj ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5bwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bwj OCA], [https://pdbe.org/5bwj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bwj RCSB], [https://www.ebi.ac.uk/pdbsum/5bwj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bwj ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/O51381_BORBU O51381_BORBU]
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Two-component signal transduction systems are the primary mechanisms by which bacteria perceive and respond to changes in their environment. The Hk1/Rrp1 two-component system (TCS) in Borrelia burgdorferi consists of a hybrid histidine kinase and a response regulator with diguanylate cyclase activity, respectively. Phosphorylated Rrp1 catalyzes the synthesis of c-di-GMP, a second messenger associated with bacterial life-style control networks. Spirochetes lacking either Hk1 or Rrp1 are virulent in mice but destroyed within feeding ticks. Activation of Hk1 by exogenous stimuli represents the seminal event for c-di-GMP signaling. We reasoned that structural characterization of Hk1's sensor would provide insights into the mechanism underlying signal transduction and aid in the identification of activating ligands. The Hk1 sensor is composed of three ligand-binding domains (D1-3), each with homology to periplasmic solute-binding proteins (PBPs) typically associated with ABC transporters. Herein, we determined the structure for D1, the most N-terminal PBP domain. As expected, D1 displays a bilobed Venus Fly Trap-fold. Similar to the prototypical sensor PBPs HK29S from Geobacter sulfurreducens and VFT2 from Bordetella pertussis, apo-D1 adopts a closed conformation. Using complementary approaches, including SAXS, we established that D1 forms a dimer in solution. The D1 structure enabled us to model the D2 and D3 domains. Differences in the ligand-binding pockets suggest that each PBP recognizes a different ligand. The ability of Hk1 to recognize multiple stimuli provides spirochetes with a means of distinguishing between the acquisition and transmission blood meals and generate a graded output response that is reflective of the perceived environmental threats.
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Structural characterization and modeling of the Borrelia burgdorferi hybrid histidine kinase Hk1 periplasmic sensor: A system for sensing small molecules associated with tick feeding.,Bauer WJ, Luthra A, Zhu G, Radolf JD, Malkowski MG, Caimano MJ J Struct Biol. 2015 Aug 28. pii: S1047-8477(15)30051-4. doi:, 10.1016/j.jsb.2015.08.013. PMID:26321039<ref>PMID:26321039</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5bwj" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Borbu]]
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[[Category: Borreliella burgdorferi B31]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bauer, W J]]
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[[Category: Bauer WJ]]
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[[Category: Caimano, M J]]
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[[Category: Caimano MJ]]
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[[Category: Luthra, A]]
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[[Category: Luthra A]]
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[[Category: Malkowski, M G]]
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[[Category: Malkowski MG]]
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[[Category: Radolf, J D]]
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[[Category: Radolf JD]]
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[[Category: Zhu, G]]
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[[Category: Zhu G]]
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[[Category: Lyme disease]]
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[[Category: Periplasmic sensor domain]]
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[[Category: Signaling protein]]
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[[Category: Venus fly trap fold]]
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Current revision

Structural characterization and modeling of the Borrelia burgdorferi hybrid histidine kinase Hk1 periplasmic sensor

PDB ID 5bwj

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