View source for 3zrx


==The high resolution structure of a dimeric Hamp-Dhp fusion displays strong asymmetry==
<StructureSection load='3zrx' size='340' side='right'caption='[[3zrx]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zrx]] 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=3ZRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZRX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.25&#8491;</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=3zrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zrx OCA], [https://pdbe.org/3zrx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zrx RCSB], [https://www.ebi.ac.uk/pdbsum/3zrx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zrx ProSAT]</span></td></tr>
</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;">
== Publication Abstract from PubMed ==
Bacterial 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<ref>PMID:22244755</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zrx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Archaeoglobus fulgidus DSM 4304]]
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Hulko M]]
[[Category: Martin J]]
[[Category: Zeth K]]