View source for 6qrj


==Crystal structure of ShkA full-length in complex with AMPPNP==
<StructureSection load='6qrj' size='340' side='right'caption='[[6qrj]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6qrj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides_CB15 Caulobacter vibrioides CB15]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QRJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QRJ 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]] 2.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6qrj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qrj OCA], [https://pdbe.org/6qrj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qrj RCSB], [https://www.ebi.ac.uk/pdbsum/6qrj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qrj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9ABT2_CAUVC Q9ABT2_CAUVC] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cytosolic hybrid histidine kinases (HHKs) constitute major signaling nodes that control various biological processes, but their input signals and how these are processed are largely unknown. In Caulobacter crescentus, the HHK ShkA is essential for accurate timing of the G1-S cell cycle transition and is regulated by the corresponding increase in the level of the second messenger c-di-GMP. Here, we use a combination of X-ray crystallography, NMR spectroscopy, functional analyses, and kinetic modeling to reveal the regulatory mechanism of ShkA. In the absence of c-di-GMP, ShkA predominantly adopts a compact domain arrangement that is catalytically inactive. C-di-GMP binds to the dedicated pseudoreceiver domain Rec1, thereby liberating the canonical Rec2 domain from its central position where it obstructs the large-scale motions required for catalysis. Thus, c-di-GMP cannot only stabilize domain interactions, but also engage in domain dissociation to allosterically invoke a downstream effect. Enzyme kinetics data are consistent with conformational selection of the ensemble of active domain constellations by the ligand and show that autophosphorylation is a reversible process.

Hybrid histidine kinase activation by cyclic di-GMP-mediated domain liberation.,Dubey BN, Agustoni E, Bohm R, Kaczmarczyk A, Mangia F, von Arx C, Jenal U, Hiller S, Plaza-Menacho I, Schirmer T Proc Natl Acad Sci U S A. 2019 Dec 27. pii: 1911427117. doi:, 10.1073/pnas.1911427117. PMID:31882446<ref>PMID:31882446</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6qrj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Caulobacter vibrioides CB15]]
[[Category: Large Structures]]
[[Category: Dubey BN]]
[[Category: Schirmer T]]