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| | <StructureSection load='3v67' size='340' side='right'caption='[[3v67]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='3v67' size='340' side='right'caption='[[3v67]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3v67]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"oceanomonas_parahaemolytica"_(fujino_et_al._1951)_miyamoto_et_al._1961 "oceanomonas parahaemolytica" (fujino et al. 1951) miyamoto et al. 1961]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V67 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3v67]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_parahaemolyticus Vibrio parahaemolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V67 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VP2859 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=670 "Oceanomonas parahaemolytica" (Fujino et al. 1951) Miyamoto et al. 1961])</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]] 2.3Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </span></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=3v67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v67 OCA], [https://pdbe.org/3v67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v67 RCSB], [https://www.ebi.ac.uk/pdbsum/3v67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v67 ProSAT]</span></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=3v67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v67 OCA], [https://pdbe.org/3v67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v67 RCSB], [https://www.ebi.ac.uk/pdbsum/3v67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v67 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Q87KW6_VIBPA Q87KW6_VIBPA] |
| - | The Cpx two-component system of Gram-negative bacteria senses extracytoplasmic stresses using the histidine kinase CpxA, a membrane-bound sensor, and controls the transcription of the genes involved in stress response by the cytosolic response regulator CpxR, which is activated by the phosphorelay from CpxA. CpxP, a CpxA-associated protein, also plays an important role in the regulation of the Cpx system by inhibiting the autophosphorylation of CpxA. Although the stress signals and physiological roles of the Cpx system have been extensively studied, the lack of structural information has limited the understanding of the detailed mechanism of ligand binding and regulation of CpxA. In this study, we solved the crystal structure of the periplasmic domain of Vibrio parahaemolyticus CpxA (VpCpxA-peri) to a resolution of 2.1 A and investigated its interaction with CpxP. VpCpxA-peri has a globular Per-ARNT-SIM (PAS) domain and a protruded C-terminal tail, which may be required for ligand sensing and CpxP binding, respectively. The direct interaction of the PAS core of VpCpxA-peri with VpCpxP was not detected by NMR, suggesting that the C-terminal tail or other factors, such as the membrane environment, are necessary for the binding of CpxA to CpxP.
| + | |
| - | | + | |
| - | The crystal structure of the periplasmic domain of Vibrio parahaemolyticus CpxA.,Kwon E, Kim DY, Ngo TD, Gross CA, Gross JD, Kim KK Protein Sci. 2012 Sep;21(9):1334-43. doi: 10.1002/pro.2120. PMID:22760860<ref>PMID:22760860</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 3v67" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Histidine kinase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gross, J D]] | + | [[Category: Vibrio parahaemolyticus]] |
| - | [[Category: Kim, D Y]] | + | [[Category: Gross JD]] |
| - | [[Category: Kim, K K]] | + | [[Category: Kim DY]] |
| - | [[Category: Kwon, E]] | + | [[Category: Kim KK]] |
| - | [[Category: Ngo, T D]] | + | [[Category: Kwon E]] |
| - | [[Category: Merohedral twinning]] | + | [[Category: Ngo TD]] |
| - | [[Category: Pas fold]]
| + | |
| - | [[Category: Signal sensing]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
