5xga

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Current revision (10:18, 27 March 2024) (edit) (undo)
 
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<StructureSection load='5xga' size='340' side='right'caption='[[5xga]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='5xga' size='340' side='right'caption='[[5xga]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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://proteopedia.org/fgij/fg.htm?mol=5XGA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5xga]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5XGA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CPS:3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE'>CPS</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]] 1.951&#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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CPS:3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE'>CPS</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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>
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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=5xga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xga OCA], [https://pdbe.org/5xga PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xga RCSB], [https://www.ebi.ac.uk/pdbsum/5xga PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xga ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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.
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[https://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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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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 5xga" 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]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cheong, C]]
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[[Category: Cheong C]]
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[[Category: Cheong, H K]]
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[[Category: Cheong HK]]
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[[Category: Hwang, E]]
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[[Category: Hwang E]]
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[[Category: Jeon, Y H]]
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[[Category: Jeon YH]]
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[[Category: Envz]]
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[[Category: Transferase]]
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Current revision

Crystal structure of the EnvZ periplasmic domain with CHAPS

PDB ID 5xga

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