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4wy9

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<StructureSection load='4wy9' size='340' side='right'caption='[[4wy9]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
<StructureSection load='4wy9' size='340' side='right'caption='[[4wy9]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4wy9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Camje Camje]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WY9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WY9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4wy9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni_subsp._jejuni_NCTC_11168_=_ATCC_700819 Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WY9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WY9 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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 1.4&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cj1506c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=192222 CAMJE])</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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=4wy9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wy9 OCA], [http://pdbe.org/4wy9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wy9 RCSB], [http://www.ebi.ac.uk/pdbsum/4wy9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wy9 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=4wy9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wy9 OCA], [https://pdbe.org/4wy9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wy9 RCSB], [https://www.ebi.ac.uk/pdbsum/4wy9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wy9 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/Q0P8B2_CAMJE Q0P8B2_CAMJE]
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Chemotaxis and motility play an important role in the colonisation of avian and human hosts by Campylobacter jejuni. Chemotactic recognition of extracellular signals is mediated by the periplasmic sensing domain of methyl-accepting chemotactic proteins (membrane-embedded receptors). In this work, we report a high-resolution structure of the periplasmic sensing domain of transducer-like protein 1 (Tlp1), an aspartate receptor of C. jejuni. Crystallographic analysis revealed that it contains two Per-Arnt-Sim (PAS) subdomains. An acetate and chloride ions (both from the crystallisation buffer) were observed bound to the membrane-proximal and membrane-distal PAS subdomains, respectively. Surprisingly, despite being crystallised in the presence of aspartate, the structure did not show any electron density corresponding to this amino acid. Furthermore, no binding between the sensing domain of Tlp1 and aspartate was detected by microcalorimetric experiments. These structural and biophysical data suggest that Tlp1 does not sense aspartate directly; instead, ligand recognition is likely to occur indirectly via an as yet unidentified periplasmic binding protein.
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The Crystal Structure of the Tandem-PAS Sensing Domain of Campylobacter jejuni Chemoreceptor Tlp1 Suggests Indirect Mechanism of Ligand Recognition.,Machuca MA, Liu YC, Beckham SA, Gunzburg MJ, Roujeinikova A J Struct Biol. 2016 Feb 23. pii: S1047-8477(16)30034-X. doi:, 10.1016/j.jsb.2016.02.019. PMID:26923153<ref>PMID:26923153</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 4wy9" 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: Camje]]
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[[Category: Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Liu, Y C]]
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[[Category: Liu YC]]
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[[Category: Machuca, M A]]
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[[Category: Machuca MA]]
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[[Category: Roujeinikova, A]]
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[[Category: Roujeinikova A]]
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[[Category: Campylobacter jejuni]]
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[[Category: Chemotaxis]]
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[[Category: Methyl-accepting protein]]
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[[Category: Sensory domain]]
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[[Category: Signaling protein]]
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[[Category: Transducer-like protein]]
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Current revision

Crystal structure of the periplasmic sensory domain of the Campylobacter jejuni chemoreceptor Tlp1

PDB ID 4wy9

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