View source for 4biu


==Crystal structure of CpxAHDC (orthorhombic form 1)==
<StructureSection load='4biu' size='340' side='right'caption='[[4biu]], [[Resolution|resolution]] 3.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4biu]] is a 6 chain structure with sequence from [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=4BIU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BIU 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]] 3.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4biu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4biu OCA], [https://pdbe.org/4biu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4biu RCSB], [https://www.ebi.ac.uk/pdbsum/4biu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4biu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CPXA_ECOLI CPXA_ECOLI] This protein is involved in several diverse cellular processes, such as the functioning of acetohydroxyacid synthetase I, in the biosynthesis of isoleucine and valine, the TraJ protein activation activity for tra gene expression in F plasmid, and the synthesis, translocation, or stability of cell envelope proteins. Activates CpxR by phosphorylation.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Histidine kinases (HKs) are dimeric receptors that participate in most adaptive responses to environmental changes in prokaryotes. Although it is well established that stimulus perception triggers autophosphorylation in many HKs, little is known on how the input signal propagates through the HAMP domain to control the transient interaction between the histidine-containing and ATP-binding domains during the catalytic reaction. Here we report crystal structures of the full cytoplasmic region of CpxA, a prototypical HK involved in Escherichia coli response to envelope stress. The structural ensemble, which includes the Michaelis complex, unveils HK activation as a highly dynamic process, in which HAMP modulates the segmental mobility of the central HK alpha-helices to promote a strong conformational and dynamical asymmetry that characterizes the kinase-active state. A mechanical model based on our structural and biochemical data provides insights into HAMP-mediated signal transduction, the autophosphorylation reaction mechanism, and the symmetry-dependent control of HK kinase/phosphatase functional states.

Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation.,Mechaly AE, Sassoon N, Betton JM, Alzari PM PLoS Biol. 2014 Jan 28;12(1):e1001776. doi: 10.1371/journal.pbio.1001776., eCollection 2014 Jan. PMID:24492262<ref>PMID:24492262</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4biu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Alzari PM]]
[[Category: Betton JM]]
[[Category: Mechaly AE]]
[[Category: Sassoon N]]