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6k62

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Current revision (10:41, 27 March 2024) (edit) (undo)
 
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<StructureSection load='6k62' size='340' side='right'caption='[[6k62]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
<StructureSection load='6k62' size='340' side='right'caption='[[6k62]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6k62]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanc8 Xanc8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K62 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6K62 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6k62]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris_str._8004 Xanthomonas campestris pv. campestris str. 8004]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K62 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K62 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XC_1756 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=314565 XANC8])</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]] 2.55&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </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=6k62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k62 OCA], [https://pdbe.org/6k62 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k62 RCSB], [https://www.ebi.ac.uk/pdbsum/6k62 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k62 ProSAT]</span></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=6k62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k62 OCA], [http://pdbe.org/6k62 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k62 RCSB], [http://www.ebi.ac.uk/pdbsum/6k62 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k62 ProSAT]</span></td></tr>
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</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/A0A0H2X6K9_XANC8 A0A0H2X6K9_XANC8]
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Plant cytokinins (CKs) are essential for many central cellular processes and play important roles in the interaction between bacteria and plants. Perception of CK is executed by the CHASE domain in the histidine kinase sensors of a class of two-component regulatory systems. Despite advances in understanding the structural basis for CK perception by the sensor AHK4 in Arabidopsis, the molecular mechanism of CK binding by other sensors is unclear. Here, we report the crystal structure of the CHASE domain in the histidine kinase PcrK of the bacterial plant pathogen Xanthomonas campestris pathovar campestris, which senses plant CK, determined at 2.55A resolution. The structure reveals that the PcrK has an AHK4-like overall topology and assembles into a homodimer. Strikingly, detailed structural analysis unveils two unique features of the PcrK ligand binding pocket: the size of the pocket is restricted for CK binding, and the PcrK applies a positively charged arginine but not a negatively charged aspartate to recognize the ligand. We propose a model to explain how the PcrK accommodates CK-sized compounds through conformational changes, providing a potential mechanistic framework for understanding ligand recognition by the PcrK.
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The crystal structure of the phytopathogenic bacterial sensor PcrK reveals different cytokinin recognition mechanism from the plant sensor AHK4.,Chen P, Jiao X, Zhang Y, Wu L, Tang DJ, Li P, Chen X, Chao D, Tang JL, Ming Z J Struct Biol. 2019 Oct 1;208(1):69-76. doi: 10.1016/j.jsb.2019.08.001. Epub 2019, Aug 13. PMID:31419523<ref>PMID:31419523</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 6k62" 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: Histidine kinase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Xanc8]]
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[[Category: Xanthomonas campestris pv. campestris str. 8004]]
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[[Category: Chen, P]]
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[[Category: Chen P]]
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[[Category: Ming, Z H]]
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[[Category: Ming ZH]]
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[[Category: Tang, J L]]
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[[Category: Tang JL]]
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[[Category: Wu, L J]]
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[[Category: Wu LJ]]
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[[Category: Cytokinin perception]]
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[[Category: Hormone]]
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Current revision

Crystal structure of Xanthomonas PcrK

PDB ID 6k62

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