3zrv: Difference between revisions
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==The high resolution structure of a dimeric Hamp-Dhp fusion displays asymmetry - A291F mutant== | ==The high resolution structure of a dimeric Hamp-Dhp fusion displays asymmetry - A291F mutant== | ||
<StructureSection load='3zrv' size='340' side='right' caption='[[3zrv]], [[Resolution|resolution]] 1.65Å' scene=''> | <StructureSection load='3zrv' size='340' side='right'caption='[[3zrv]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3zrv]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3zrv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus_DSM_4304 Archaeoglobus fulgidus DSM 4304] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZRV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZRV FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3zrv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zrv OCA], [https://pdbe.org/3zrv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zrv RCSB], [https://www.ebi.ac.uk/pdbsum/3zrv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zrv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/O28769_ARCFU O28769_ARCFU] [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. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Archaeoglobus fulgidus DSM 4304]] | ||
[[Category: | [[Category: Escherichia coli K-12]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Ferris HU]] | ||
[[Category: | [[Category: Hulko M]] | ||
[[Category: | [[Category: Martin J]] | ||
[[Category: | [[Category: Zeth K]] | ||
Latest revision as of 13:42, 9 May 2024
The high resolution structure of a dimeric Hamp-Dhp fusion displays asymmetry - A291F mutantThe high resolution structure of a dimeric Hamp-Dhp fusion displays asymmetry - A291F mutant
Structural highlights
FunctionO28769_ARCFU 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. Publication Abstract from PubMedBacterial transmembrane receptors regulate an intracellular catalytic output in response to extracellular sensory input. To investigate the conformational changes that relay the regulatory signal, we have studied the HAMP domain, a ubiquitous intracellular module connecting input to output domains. HAMP forms a parallel, dimeric, four-helical coiled coil, and rational substitutions in our model domain (Af1503 HAMP) induce a transition in its interhelical packing, characterized by axial rotation of all four helices (the gearbox signaling model). We now illustrate how these conformational changes are propagated to a downstream domain by fusing Af1503 HAMP variants to the DHp domain of EnvZ, a bacterial histidine kinase. Structures of wild-type and mutant constructs are correlated with ligand response in vivo, clearly associating them with distinct signaling states. We propose that altered recognition of the catalytic domain by DHp, rather than a shift in position of the phospho-accepting histidine, forms the basis for regulation of kinase activity. Mechanism of regulation of receptor histidine kinases.,Ferris HU, Dunin-Horkawicz S, Hornig N, Hulko M, Martin J, Schultz JE, Zeth K, Lupas AN, Coles M Structure. 2012 Jan 11;20(1):56-66. PMID:22244755[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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