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| | ==Bifunctional histidine kinase CckA (domains DHp-CA) in complex with ADP/Mg2+== | | ==Bifunctional histidine kinase CckA (domains DHp-CA) in complex with ADP/Mg2+== |
| - | <StructureSection load='5idj' size='340' side='right' caption='[[5idj]], [[Resolution|resolution]] 3.01Å' scene=''> | + | <StructureSection load='5idj' size='340' side='right'caption='[[5idj]], [[Resolution|resolution]] 3.02Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5idj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cauvi Cauvi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IDJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IDJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5idj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IDJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IDJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 3.02Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cckA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155892 CAUVI])</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=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <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=5idj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5idj OCA], [http://pdbe.org/5idj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5idj RCSB], [http://www.ebi.ac.uk/pdbsum/5idj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5idj ProSAT]</span></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=5idj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5idj OCA], [https://pdbe.org/5idj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5idj RCSB], [https://www.ebi.ac.uk/pdbsum/5idj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5idj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Q9X688_CAUVI Q9X688_CAUVI] |
| - | Histidine kinases are key components of regulatory networks in bacteria. Although many of these enzymes are bifunctional, mediating both phosphorylation and dephosphorylation of downstream targets, the molecular details of this central regulatory switch are unclear. We showed recently that the universal second messenger cyclic di-guanosine monophosphate (c-di-GMP) drives Caulobacter crescentus cell cycle progression by forcing the cell cycle kinase CckA from its default kinase into phosphatase mode. We use a combination of structure determination, modeling, and functional analysis to demonstrate that c-di-GMP reciprocally regulates the two antagonistic CckA activities through noncovalent cross-linking of the catalytic domain with the dimerization histidine phosphotransfer (DHp) domain. We demonstrate that both c-di-GMP and ADP (adenosine diphosphate) promote phosphatase activity and propose that c-di-GMP stabilizes the ADP-bound quaternary structure, which allows the receiver domain to access the dimeric DHp stem for dephosphorylation. In silico analyses predict that c-di-GMP control is widespread among bacterial histidine kinases, arguing that it can replace or modulate canonical transmembrane signaling.
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| - | Cyclic di-GMP mediates a histidine kinase/phosphatase switch by noncovalent domain cross-linking.,Dubey BN, Lori C, Ozaki S, Fucile G, Plaza-Menacho I, Jenal U, Schirmer T Sci Adv. 2016 Sep 16;2(9):e1600823. doi: 10.1126/sciadv.1600823. eCollection 2016, Sep. PMID:27652341<ref>PMID:27652341</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 5idj" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cauvi]] | + | [[Category: Caulobacter vibrioides]] |
| - | [[Category: Dubey, B N]] | + | [[Category: Large Structures]] |
| - | [[Category: Schirmer, T]] | + | [[Category: Dubey BN]] |
| - | [[Category: Bifunctional]] | + | [[Category: Schirmer T]] |
| - | [[Category: Histidine kinase]]
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| - | [[Category: Phosphatase]]
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| - | [[Category: Transferase]]
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