5iul: Difference between revisions

Revision as of 21:41, 22 December 2016

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. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	ACP, K, MG
Related:	5iuj, 5iuk, 5ium, 5iun
Activity:	Histidine kinase, with EC number 2.7.13.3
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] [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.^[6] ^[7] ^[8] ^[9] ^[10]

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
↑ 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

Proteopedia Page Contributors and Editors (what is this?)

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

[6] 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

[7] 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

[8] 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

[9] 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

[10] 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=''>
-Authors: Trajtenberg, F., Imelio, J.A., Larrieux, N., Buschiazzo, A.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5iul]] is a 6 chain structure. 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>
-Description: Crystal structure of the DesK-DesR complex in the phosphotransfer state with high Mg2+ (150 mM) and BeF3
+</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>
-[[Category: Unreleased Structures]]
+<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='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>
+== 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>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Histidine kinase]]
+[[Category: Buschiazzo, A]]
+[[Category: Imelio, J A]]
 [[Category: Larrieux, N]]
-[[Category: Imelio, J.A]]
-[[Category: Buschiazzo, A]]
 [[Category: Trajtenberg, F]]
+[[Category: Kinase]]
+[[Category: Phosphotransfer]]
+[[Category: Phosphotransfer complex]]
+[[Category: Response regulator]]
+[[Category: Transferase]]
+[[Category: Two-component regulatory system]]

5iul: Difference between revisions

Revision as of 21:41, 22 December 2016

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

Structural highlights

Function

References

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