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| | ==Crystal structure of the DesK-DesR complex in the phosphotransfer state with high Mg2+ (150 mM) and BeF3== | | ==Crystal structure of the DesK-DesR complex in the phosphotransfer state with high Mg2+ (150 mM) and BeF3== |
| - | <StructureSection load='5iul' size='340' side='right' caption='[[5iul]], [[Resolution|resolution]] 3.15Å' scene=''> | + | <StructureSection load='5iul' size='340' side='right'caption='[[5iul]], [[Resolution|resolution]] 3.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5iul]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IUL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IUL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5iul]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IUL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IUL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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]] 3.153Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5iuj|5iuj]], [[5iuk|5iuk]], [[5ium|5ium]], [[5iun|5iun]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">desK, yocF, BSU19190 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU]), desR, yocG, BSU19200 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</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=5iul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iul OCA], [https://pdbe.org/5iul PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iul RCSB], [https://www.ebi.ac.uk/pdbsum/5iul PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iul ProSAT]</span></td></tr> |
| - | <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> | + | |
| - | <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=5iul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iul OCA], [http://pdbe.org/5iul PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5iul RCSB], [http://www.ebi.ac.uk/pdbsum/5iul PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5iul ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DESK_BACSU DESK_BACSU]] Member of the two-component regulatory system DesR/DesK, responsible for cold induction of the des gene coding for the Delta5 acyl-lipid desaturase. Acts as a sensor of the membrane fluidity. Probably activates DesR by phosphorylation.<ref>PMID:11285232</ref> <ref>PMID:11717295</ref> <ref>PMID:12207704</ref> <ref>PMID:14734164</ref> <ref>PMID:15090506</ref> [[http://www.uniprot.org/uniprot/DESR_BACSU DESR_BACSU]] Member of the two-component regulatory system DesR/DesK, responsible for cold induction of the des gene coding for the Delta5 acyl-lipid desaturase.<ref>PMID:11285232</ref> <ref>PMID:11717295</ref> <ref>PMID:12207704</ref> <ref>PMID:14734164</ref> <ref>PMID:15090506</ref> | + | [https://www.uniprot.org/uniprot/DESK_BACSU DESK_BACSU] Member of the two-component regulatory system DesR/DesK, responsible for cold induction of the des gene coding for the Delta5 acyl-lipid desaturase. Acts as a sensor of the membrane fluidity. Probably activates DesR by phosphorylation.<ref>PMID:11285232</ref> <ref>PMID:11717295</ref> <ref>PMID:12207704</ref> <ref>PMID:14734164</ref> <ref>PMID:15090506</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5iul" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5iul" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Response regulator 3D structure|Response regulator 3D structure]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacsu]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| - | [[Category: Histidine kinase]] | + | [[Category: Large Structures]] |
| - | [[Category: Buschiazzo, A]] | + | [[Category: Buschiazzo A]] |
| - | [[Category: Imelio, J A]] | + | [[Category: Imelio JA]] |
| - | [[Category: Larrieux, N]] | + | [[Category: Larrieux N]] |
| - | [[Category: Trajtenberg, F]] | + | [[Category: Trajtenberg F]] |
| - | [[Category: Kinase]]
| + | |
| - | [[Category: Phosphotransfer]]
| + | |
| - | [[Category: Phosphotransfer complex]]
| + | |
| - | [[Category: Response regulator]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Two-component regulatory system]]
| + | |
| Structural highlights
Function
DESK_BACSU Member of the two-component regulatory system DesR/DesK, responsible for cold induction of the des gene coding for the Delta5 acyl-lipid desaturase. Acts as a sensor of the membrane fluidity. Probably activates DesR by phosphorylation.[1] [2] [3] [4] [5]
Publication Abstract from PubMed
Two-component systems (TCS) are protein machineries that enable cells to respond to input signals. Histidine kinases (HK) are the sensory component, transferring information toward downstream response regulators (RR). HKs transfer phosphoryl groups to their specific RRs, but also dephosphorylate them, overall ensuring proper signaling. The mechanisms by which HKs discriminate between such disparate directions, are yet unknown. We now disclose crystal structures of the HK:RR complex DesK:DesR from Bacillus subtilis, comprising snapshots of the phosphotransfer and the dephosphorylation reactions. The HK dictates the reactional outcome through conformational rearrangements that include the reactive histidine. The phosphotransfer center is asymmetric, poised for dissociative nucleophilic substitution. The structural bases of HK phosphatase/phosphotransferase control are uncovered, and the unexpected discovery of a dissociative reactional center, sheds light on the evolution of TCS phosphotransfer reversibility. Our findings should be applicable to a broad range of signaling systems and instrumental in synthetic TCS rewiring.
Regulation of signaling directionality revealed by 3D snapshots of a kinase:regulator complex in action.,Trajtenberg F, Imelio JA, Machado MR, Larrieux N, Marti MA, Obal G, Mechaly AE, Buschiazzo A Elife. 2016 Dec 12;5. pii: e21422. doi: 10.7554/eLife.21422. PMID:27938660[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Aguilar PS, Hernandez-Arriaga AM, Cybulski LE, Erazo AC, de Mendoza D. Molecular basis of thermosensing: a two-component signal transduction thermometer in Bacillus subtilis. EMBO J. 2001 Apr 2;20(7):1681-91. PMID:11285232 doi:http://dx.doi.org/10.1093/emboj/20.7.1681
- ↑ Kobayashi K, Ogura M, Yamaguchi H, Yoshida K, Ogasawara N, Tanaka T, Fujita Y. Comprehensive DNA microarray analysis of Bacillus subtilis two-component regulatory systems. J Bacteriol. 2001 Dec;183(24):7365-70. PMID:11717295 doi:http://dx.doi.org/10.1128/JB.183.24.7365-7370.2001
- ↑ Cybulski LE, Albanesi D, Mansilla MC, Altabe S, Aguilar PS, de Mendoza D. Mechanism of membrane fluidity optimization: isothermal control of the Bacillus subtilis acyl-lipid desaturase. Mol Microbiol. 2002 Sep;45(5):1379-88. PMID:12207704
- ↑ Hunger K, Beckering CL, Marahiel MA. Genetic evidence for the temperature-sensing ability of the membrane domain of the Bacillus subtilis histidine kinase DesK. FEMS Microbiol Lett. 2004 Jan 15;230(1):41-6. PMID:14734164
- ↑ Albanesi D, Mansilla MC, de Mendoza D. The membrane fluidity sensor DesK of Bacillus subtilis controls the signal decay of its cognate response regulator. J Bacteriol. 2004 May;186(9):2655-63. PMID:15090506
- ↑ Trajtenberg F, Imelio JA, Machado MR, Larrieux N, Marti MA, Obal G, Mechaly AE, Buschiazzo A. Regulation of signaling directionality revealed by 3D snapshots of a kinase:regulator complex in action. Elife. 2016 Dec 12;5. pii: e21422. doi: 10.7554/eLife.21422. PMID:27938660 doi:http://dx.doi.org/10.7554/eLife.21422
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