5iul: Difference between revisions

Latest revision as of 12:35, 6 March 2024

Crystal structure of the DesK-DesR complex in the phosphotransfer state with high Mg2+ (150 mM) and BeF3

Structural highlights

5iul 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 3.153Å
Ligands:	ACP, K, MG
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]

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:https://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:https://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

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OCA

[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:https://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:https://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

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5iul is ON HOLD  until Paper Publication
+==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]] 3.15&Aring;' scene=''>
+== Structural highlights ==
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.153&#8491;</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='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>
+</table>
+== Function ==
+[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>
-Authors: Trajtenberg, F., Imelio, J.A., Larrieux, N., Buschiazzo, A.
+==See Also==
+*[[Response regulator 3D structure|Response regulator 3D structure]]
-Description: Crystal structure of the DesK-DesR complex in the phosphotransfer state with high Mg2+ (150 mM) and BeF3
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
-[[Category: Larrieux, N]]
+__TOC__
-[[Category: Imelio, J.A]]
+</StructureSection>
-[[Category: Buschiazzo, A]]
+[[Category: Bacillus subtilis subsp. subtilis str. 168]]
-[[Category: Trajtenberg, F]]
+[[Category: Large Structures]]
+[[Category: Buschiazzo A]]
+[[Category: Imelio JA]]
+[[Category: Larrieux N]]
+[[Category: Trajtenberg F]]

5iul: Difference between revisions

Latest revision as of 12:35, 6 March 2024

Crystal structure of the DesK-DesR complex in the phosphotransfer state with high Mg2+ (150 mM) and BeF3

Structural highlights

Function

See Also

References

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