2bnl

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[[Image:2bnl.png|left|200px]]
 
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{{STRUCTURE_2bnl| PDB=2bnl | SCENE= }}
{{STRUCTURE_2bnl| PDB=2bnl | SCENE= }}
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===THE STRUCTURE OF THE N-TERMINAL DOMAIN OF RSBR===
===THE STRUCTURE OF THE N-TERMINAL DOMAIN OF RSBR===
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{{ABSTRACT_PUBMED_16301540}}
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==Function==
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[[http://www.uniprot.org/uniprot/RSBR_BACSU RSBR_BACSU]] Acts as a positive regulator of sigma-B activity in response to salt and heat stress by stimulating the activity of the RsbT kinase toward RsbS in vitro.<ref>PMID:11157946</ref> <ref>PMID:15312768</ref> One of 4 functionally non-identical RsbR paralogs, it functions in the environmental signaling branch of the general stress response.<ref>PMID:11157946</ref> <ref>PMID:15312768</ref> Negative regulator of sigma-B activity. Non-phosphorylated RsbS binds to RsbT, preventing its association with RsbU. Requires any one of RsbRA, RsbRB, RsbRC or RsbRD to sequester RsbT. When RsbS and the RsbR paralog(s) are phosphorylated, they release RsbT, which can then bind and activate RsbU.<ref>PMID:11157946</ref> <ref>PMID:15312768</ref>
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{{ABSTRACT_PUBMED_16301540}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:016301540</ref><references group="xtra"/>
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<ref group="xtra">PMID:016301540</ref><references group="xtra"/><references/>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Delumeau, O.]]
[[Category: Delumeau, O.]]

Revision as of 08:18, 23 April 2014

Template:STRUCTURE 2bnl

Contents

THE STRUCTURE OF THE N-TERMINAL DOMAIN OF RSBR

Template:ABSTRACT PUBMED 16301540

Function

[RSBR_BACSU] Acts as a positive regulator of sigma-B activity in response to salt and heat stress by stimulating the activity of the RsbT kinase toward RsbS in vitro.[1] [2] One of 4 functionally non-identical RsbR paralogs, it functions in the environmental signaling branch of the general stress response.[3] [4] Negative regulator of sigma-B activity. Non-phosphorylated RsbS binds to RsbT, preventing its association with RsbU. Requires any one of RsbRA, RsbRB, RsbRC or RsbRD to sequester RsbT. When RsbS and the RsbR paralog(s) are phosphorylated, they release RsbT, which can then bind and activate RsbU.[5] [6]

About this Structure

2bnl is a 6 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

  • Murray JW, Delumeau O, Lewis RJ. Structure of a nonheme globin in environmental stress signaling. Proc Natl Acad Sci U S A. 2005 Nov 29;102(48):17320-5. Epub 2005 Nov 21. PMID:16301540
  1. Akbar S, Gaidenko TA, Kang CM, O'Reilly M, Devine KM, Price CW. New family of regulators in the environmental signaling pathway which activates the general stress transcription factor sigma(B) of Bacillus subtilis. J Bacteriol. 2001 Feb;183(4):1329-38. PMID:11157946 doi:10.1128/JB.183.4.1329-1338.2001
  2. Kim TJ, Gaidenko TA, Price CW. A multicomponent protein complex mediates environmental stress signaling in Bacillus subtilis. J Mol Biol. 2004 Jul 30;341(1):135-50. PMID:15312768 doi:http://dx.doi.org/10.1016/j.jmb.2004.05.043
  3. Akbar S, Gaidenko TA, Kang CM, O'Reilly M, Devine KM, Price CW. New family of regulators in the environmental signaling pathway which activates the general stress transcription factor sigma(B) of Bacillus subtilis. J Bacteriol. 2001 Feb;183(4):1329-38. PMID:11157946 doi:10.1128/JB.183.4.1329-1338.2001
  4. Kim TJ, Gaidenko TA, Price CW. A multicomponent protein complex mediates environmental stress signaling in Bacillus subtilis. J Mol Biol. 2004 Jul 30;341(1):135-50. PMID:15312768 doi:http://dx.doi.org/10.1016/j.jmb.2004.05.043
  5. Akbar S, Gaidenko TA, Kang CM, O'Reilly M, Devine KM, Price CW. New family of regulators in the environmental signaling pathway which activates the general stress transcription factor sigma(B) of Bacillus subtilis. J Bacteriol. 2001 Feb;183(4):1329-38. PMID:11157946 doi:10.1128/JB.183.4.1329-1338.2001
  6. Kim TJ, Gaidenko TA, Price CW. A multicomponent protein complex mediates environmental stress signaling in Bacillus subtilis. J Mol Biol. 2004 Jul 30;341(1):135-50. PMID:15312768 doi:http://dx.doi.org/10.1016/j.jmb.2004.05.043

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