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4q20

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==Crystal structure of a C-terminal part of tyrosine kinase (DivL) from Caulobacter crescentus CB15 at 2.50 A resolution (PSI Community Target, Shapiro)==
==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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<StructureSection load='4q20' size='340' side='right' caption='[[4q20]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<StructureSection load='4q20' size='340' side='right'caption='[[4q20]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4q20]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caucr Caucr]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q20 FirstGlance]. <br>
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<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>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">divL, CC_3484 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=190650 CAUCR])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </span></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q20 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q20 RCSB], [http://www.ebi.ac.uk/pdbsum/4q20 PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/DIVL_CAUCR DIVL_CAUCR]] Required for cell division and growth. It catalyzes the phosphorylation of CtrA and activates transcription in vitro of the cell cycle-regulated fliF promoter.
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Caucr]]
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[[Category: Caulobacter vibrioides CB15]]
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[[Category: Histidine kinase]]
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[[Category: Large Structures]]
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[[Category: Structural genomic]]
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[[Category: Ghkl domain]]
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[[Category: Hiska domain]]
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[[Category: Jcsg]]
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[[Category: PSI, Protein structure initiative]]
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[[Category: Psi-biology]]
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[[Category: Signal transduction]]
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[[Category: Transferase]]
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[[Category: Two-component regulatory system]]
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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)

PDB ID 4q20

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