4fmt: Difference between revisions
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==Crystal structure of a ChpT protein (CC_3470) from Caulobacter crescentus CB15 at 2.30 A resolution== | |||
<StructureSection load='4fmt' size='340' side='right'caption='[[4fmt]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4fmt]] is a 4 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=4FMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FMT 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]] 2.3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=4fmt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fmt OCA], [https://pdbe.org/4fmt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fmt RCSB], [https://www.ebi.ac.uk/pdbsum/4fmt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fmt ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9A2T6_CAUVC Q9A2T6_CAUVC] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Vital to bacterial survival is the faithful propagation of cellular signals, and in Caulobacter crescentus, ChpT is an essential mediator within the cell-cycle circuit. ChpT functions as a histidine-containing phosphotransfer protein (HPt) that shuttles a phosphoryl group from the receiver domain of CckA, the upstream hybrid histidine kinase (HK), to one of two downstream response regulators (CtrA or CpdR) that controls cell-cycle progression. To understand how ChpT interacts with multiple signaling partners, we solved the crystal structure of ChpT at 2.3 A resolution. ChpT adopts a pseudo-HK architecture but does not bind ATP. We identified two point mutation classes affecting phosphotransfer and cell morphology: one that globally impairs ChpT phosphotransfer, and a second that mediates partner selection. Importantly, a small set of conserved ChpT residues promotes signaling crosstalk and contributes to the branched signaling that activates the master regulator CtrA while inactivating the CtrA degradation signal, CpdR. | |||
Branched signal wiring of an essential bacterial cell-cycle phosphotransfer protein.,Blair JA, Xu Q, Childers WS, Mathews II, Kern JW, Eckart M, Deacon AM, Shapiro L Structure. 2013 Sep 3;21(9):1590-601. doi: 10.1016/j.str.2013.06.024. Epub 2013, Aug 8. PMID:23932593<ref>PMID:23932593</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4fmt" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Caulobacter vibrioides CB15]] | |||
[[Category: Large Structures]] | |||
[[Category: Shapiro L]] | |||
Latest revision as of 09:48, 22 May 2024
Crystal structure of a ChpT protein (CC_3470) from Caulobacter crescentus CB15 at 2.30 A resolution
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