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5xga
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the EnvZ periplasmic domain with CHAPS== | |
| + | <StructureSection load='5xga' size='340' side='right' caption='[[5xga]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5xga]] is a 1 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5dcj 5dcj]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XGA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XGA FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CPS:3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE'>CPS</scene></td></tr> | ||
| + | <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> | ||
| + | <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=5xga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xga OCA], [http://pdbe.org/5xga PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xga RCSB], [http://www.ebi.ac.uk/pdbsum/5xga PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xga ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ENVZ_ECOLI ENVZ_ECOLI]] Member of the two-component regulatory system EnvZ/OmpR involved in the regulation of osmoregulation (genes ompF and ompC). EnvZ functions as a membrane-associated protein kinase that phosphorylates OmpR in response to environmental signals. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacteria sense and respond to osmolarity through the EnvZ-OmpR two-component system. The structure of the periplasmic sensor domain of EnvZ (EnvZ-PD) is not available yet. Here, we present the crystal structure of EnvZ-PD in the presence of CHAPS detergent. The structure of EnvZ-PD shows similar folding topology to the PDC domains of PhoQ, DcuS, and CitA, but distinct orientations of helices and beta-hairpin structures. The CD and NMR spectra of EnvZ-PD in the presence of cholate, a major component of bile salts, are similar to those with CHAPS. Chemical cross-linking shows that the dimerization of EnvZ-PD is significantly inhibited by the CHAPS and cholate. Together with beta-galactosidase assay, these results suggest that bile salts may affect the EnvZ structure and function in Escherichia coli. | ||
| - | + | Crystal structure of the EnvZ periplasmic domain with CHAPS.,Hwang E, Cheong HK, Kim SY, Kwon O, Blain KY, Choe S, Yeo KJ, Jung YW, Jeon YH, Cheong C FEBS Lett. 2017 May;591(10):1419-1428. doi: 10.1002/1873-3468.12658. Epub 2017, May 9. PMID:28423182<ref>PMID:28423182</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5xga" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Histidine kinase]] | ||
[[Category: Cheong, C]] | [[Category: Cheong, C]] | ||
| - | [[Category: | + | [[Category: Cheong, H K]] |
[[Category: Hwang, E]] | [[Category: Hwang, E]] | ||
| - | [[Category: | + | [[Category: Jeon, Y H]] |
| + | [[Category: Envz]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 04:01, 30 August 2017
Crystal structure of the EnvZ periplasmic domain with CHAPS
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Categories: Histidine kinase | Cheong, C | Cheong, H K | Hwang, E | Jeon, Y H | Envz | Transferase
