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3ehg

From Proteopedia

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[[Image:3ehg.png|left|200px]]
 
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{{STRUCTURE_3ehg| PDB=3ehg | SCENE= }}
{{STRUCTURE_3ehg| PDB=3ehg | SCENE= }}
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===Crystal structure of the ATP-binding domain of DesK in complex with ATP===
===Crystal structure of the ATP-binding domain of DesK in complex with ATP===
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{{ABSTRACT_PUBMED_20507988}}
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{{ABSTRACT_PUBMED_20507988}}
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==Function==
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[[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>
==About this Structure==
==About this Structure==
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[[3ehg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EHG OCA].
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[[3ehg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EHG OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:020507988</ref><references group="xtra"/>
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<ref group="xtra">PMID:020507988</ref><references group="xtra"/><references/>
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[[Category: Bacillus subtilis]]
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[[Category: Bacillus globigii migula 1900]]
[[Category: Histidine kinase]]
[[Category: Histidine kinase]]
[[Category: Buschiazzo, A.]]
[[Category: Buschiazzo, A.]]

Revision as of 07:56, 5 February 2014

Template:STRUCTURE 3ehg

Contents

Crystal structure of the ATP-binding domain of DesK in complex with ATP

Template:ABSTRACT PUBMED 20507988

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]

About this Structure

3ehg is a 1 chain structure with sequence from "bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900. Full crystallographic information is available from OCA.

Reference

  • Trajtenberg F, Grana M, Ruetalo N, Botti H, Buschiazzo A. Structural and enzymatic insights into the ATP binding and autophosphorylation mechanism of a sensor histidine kinase. J Biol Chem. 2010 Aug 6;285(32):24892-903. Epub 2010 May 27. PMID:20507988 doi:10.1074/jbc.M110.147843
  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

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