7f2h
From Proteopedia
(Difference between revisions)
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==Crystal structure of the sensor domain of VbrK from Vibrio rotiferianus (crystal type 2)== | ==Crystal structure of the sensor domain of VbrK from Vibrio rotiferianus (crystal type 2)== | ||
| - | <StructureSection load='7f2h' size='340' side='right'caption='[[7f2h]]' scene=''> | + | <StructureSection load='7f2h' size='340' side='right'caption='[[7f2h]], [[Resolution|resolution]] 2.25Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7F2H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F2H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7f2h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_rotiferianus Vibrio rotiferianus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7F2H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F2H FirstGlance]. <br> |
| - | </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=7f2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f2h OCA], [https://pdbe.org/7f2h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f2h RCSB], [https://www.ebi.ac.uk/pdbsum/7f2h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f2h ProSAT]</span></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]] 2.25Å</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=7f2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f2h OCA], [https://pdbe.org/7f2h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f2h RCSB], [https://www.ebi.ac.uk/pdbsum/7f2h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f2h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A2K7STF1_9VIBR A0A2K7STF1_9VIBR] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Vibrio species are prevalent in the aquatic environments and can infect humans and aquatic organisms. Vibrio parahaemolyticus counteracts beta-lactam antibiotics and enhances virulence using a regulation mechanism mediated by a two-component regulatory system (TCS) consisting of the VbrK histidine kinase and the VbrR response regulator. The periplasmic sensor domain of VbrK (VbrK(SD)) detects beta-lactam antibiotics or undergoes S-nitrosylation in response to host nitrites. Although V. parahaemolyticus VbrK(SD) (vpVbrK(SD)) has recently been characterized through structural studies, it is unclear whether its structural features that are indispensable for biological functions are conserved in other VbrK orthologs. To structurally define the functionally critical regions of VbrK and address the structural dynamics of VbrK, we determined the crystal structures of Vibrio rotiferianus VbrK(SD) (vrVbrK(SD)) in two crystal forms and performed a comparative analysis of diverse VbrK structures. vrVbrK(SD) folds into a curved rod-shaped two-domain structure as observed in vpVbrK(SD). The membrane-distal end of the vrVbrK(SD) structure, including the alpha3 helix and its neighboring loops, harbors both S-nitrosylation and antibiotic-sensing sites and displays high structural flexibility and diversity. Noticeably, the distal end is partially stabilized by a disulfide bond, which is formed by the cysteine residue that is S-nitrosylated in response to nitrite. Therefore, the distal end of VbrK(SD) plays a key role in initiating the VbrK-VbrR TCS pathway activation, and it is involved in the nitrosylation-mediated regulation of the structural dynamics of VbrK. | ||
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| + | Crystal structure of the antibiotic- and nitrite-responsive histidine kinase VbrK sensor domain from Vibrio rotiferianus.,Cho SY, Yoon SI Biochem Biophys Res Commun. 2021 Sep 3;568:136-142. doi:, 10.1016/j.bbrc.2021.06.076. Epub 2021 Jun 30. PMID:34214877<ref>PMID:34214877</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7f2h" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Vibrio rotiferianus]] | ||
[[Category: Cho SY]] | [[Category: Cho SY]] | ||
[[Category: Yoon SI]] | [[Category: Yoon SI]] | ||
Current revision
Crystal structure of the sensor domain of VbrK from Vibrio rotiferianus (crystal type 2)
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