4q20
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4q20]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides_CB15 Caulobacter vibrioides CB15]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ew8 4ew8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q20 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q20 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4q20]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides_CB15 Caulobacter vibrioides CB15]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ew8 4ew8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q20 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q20 FirstGlance]. <br> | ||
| - | </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=4q20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q20 OCA], [https://pdbe.org/4q20 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q20 RCSB], [https://www.ebi.ac.uk/pdbsum/4q20 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q20 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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=4q20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q20 OCA], [https://pdbe.org/4q20 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q20 RCSB], [https://www.ebi.ac.uk/pdbsum/4q20 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q20 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/DIVL_CAUVC DIVL_CAUVC] Required for cell division and growth. It catalyzes the phosphorylation of CtrA and activates transcription in vitro of the cell cycle-regulated fliF promoter. | [https://www.uniprot.org/uniprot/DIVL_CAUVC DIVL_CAUVC] Required for cell division and growth. It catalyzes the phosphorylation of CtrA and activates transcription in vitro of the cell cycle-regulated fliF promoter. | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | One of the simplest organisms to divide asymmetrically is the bacterium Caulobacter crescentus. The DivL pseudo-histidine kinase, positioned at one cell pole, regulates cell-fate by controlling the activation of the global transcription factor CtrA via an interaction with the response regulator (RR) DivK. DivL uniquely contains a tyrosine at the histidine phosphorylation site, and can achieve these regulatory functions in vivo without kinase activity. Determination of the DivL crystal structure and biochemical analysis of wild-type and site-specific DivL mutants revealed that the DivL PAS domains regulate binding specificity for DivK approximately P over DivK, which is modulated by an allosteric intramolecular interaction between adjacent domains. We discovered that DivL's catalytic domains have been repurposed as a phosphospecific RR input sensor, thereby reversing the flow of information observed in conventional histidine kinase (HK)-RR systems and coupling a complex network of signaling proteins for cell-fate regulation. | ||
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| - | Cell fate regulation governed by a repurposed bacterial histidine kinase.,Childers WS, Xu Q, Mann TH, Mathews II, Blair JA, Deacon AM, Shapiro L PLoS Biol. 2014 Oct 28;12(10):e1001979. doi: 10.1371/journal.pbio.1001979., eCollection 2014 Oct. PMID:25349992<ref>PMID:25349992</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4q20" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Caulobacter vibrioides CB15]] | [[Category: Caulobacter vibrioides CB15]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
Current revision
Crystal structure of a C-terminal part of tyrosine kinase (DivL) from Caulobacter crescentus CB15 at 2.50 A resolution (PSI Community Target, Shapiro)
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