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==Crystal structure of the DesK-DesR complex in the phosphotransfer state with low Mg2+ (20 mM)==
==Crystal structure of the DesK-DesR complex in the phosphotransfer state with low Mg2+ (20 mM)==
<StructureSection load='5iuj' size='340' side='right' caption='[[5iuj]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='5iuj' size='340' side='right'caption='[[5iuj]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5iuj]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IUJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[5iuj]] 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=5IUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IUJ 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]] 3.2&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5iuk|5iuk]], [[5iul|5iul]], [[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='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'>[https://proteopedia.org/fgij/fg.htm?mol=5iuj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iuj OCA], [https://pdbe.org/5iuj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iuj RCSB], [https://www.ebi.ac.uk/pdbsum/5iuj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iuj ProSAT]</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=5iuj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iuj OCA], [http://pdbe.org/5iuj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5iuj RCSB], [http://www.ebi.ac.uk/pdbsum/5iuj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5iuj 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>  
 
==See Also==
*[[Response regulator 3D structure|Response regulator 3D structure]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Histidine kinase]]
[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Buschiazzo, A]]
[[Category: Large Structures]]
[[Category: Imelio, J A]]
[[Category: Buschiazzo A]]
[[Category: Larrieux, N]]
[[Category: Imelio JA]]
[[Category: Trajtenberg, F]]
[[Category: Larrieux N]]
[[Category: Kinase]]
[[Category: Trajtenberg F]]
[[Category: Phosphotransfer]]
[[Category: Phosphotransfer complex]]
[[Category: Response regulator]]
[[Category: Transferase]]
[[Category: Two-component regulatory system]]

Latest revision as of 15:35, 6 March 2024

Crystal structure of the DesK-DesR complex in the phosphotransfer state with low Mg2+ (20 mM)Crystal structure of the DesK-DesR complex in the phosphotransfer state with low Mg2+ (20 mM)

Structural highlights

5iuj is a 6 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

See Also

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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

5iuj, resolution 3.20Å

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