3zkc
From Proteopedia
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{{STRUCTURE_3zkc| PDB=3zkc | SCENE= }} | {{STRUCTURE_3zkc| PDB=3zkc | SCENE= }} | ||
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===Crystal structure of the master regulator for biofilm formation SinR in complex with DNA.=== | ===Crystal structure of the master regulator for biofilm formation SinR in complex with DNA.=== | ||
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{{ABSTRACT_PUBMED_23430750}} | {{ABSTRACT_PUBMED_23430750}} | ||
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| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/SINR_BACSU SINR_BACSU]] Negative as well as positive regulator of alternate developmental processes that are induced at the end of vegetative growth in response to nutrient depletion. Binds to the alkaline protease (aprE) gene at two sites. Also acts as a repressor of the key sporulation gene spo0A. Negatively regulates transcription of the eps operon, which is responsible for the biosynthesis of an exopolysaccharide involved in biofilm formation; therefore it could govern the transition between a state in which bacteria swim or swarm and a state in which bacteria assemble into multicellular communities. Acts with Hpr as a corepressor of epr expression. Also negatively regulates transcription of the lutABC operon, which is required for lactate utilization. Repressor activity is regulated by SinI.<ref>PMID:1898931</ref> <ref>PMID:7642487</ref> <ref>PMID:15661000</ref> <ref>PMID:16923912</ref> | ||
==About this Structure== | ==About this Structure== | ||
[[3zkc]] is a 4 chain structure with sequence from [http://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=3ZKC OCA]. | [[3zkc]] is a 4 chain structure with sequence from [http://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=3ZKC OCA]. | ||
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| + | ==Reference== | ||
| + | <references group="xtra"/><references/> | ||
[[Category: Bacillus subtilis subsp. subtilis str. 168]] | [[Category: Bacillus subtilis subsp. subtilis str. 168]] | ||
[[Category: Lewis, R J.]] | [[Category: Lewis, R J.]] | ||
Revision as of 06:42, 2 May 2013
Contents |
Crystal structure of the master regulator for biofilm formation SinR in complex with DNA.
Template:ABSTRACT PUBMED 23430750
Function
[SINR_BACSU] Negative as well as positive regulator of alternate developmental processes that are induced at the end of vegetative growth in response to nutrient depletion. Binds to the alkaline protease (aprE) gene at two sites. Also acts as a repressor of the key sporulation gene spo0A. Negatively regulates transcription of the eps operon, which is responsible for the biosynthesis of an exopolysaccharide involved in biofilm formation; therefore it could govern the transition between a state in which bacteria swim or swarm and a state in which bacteria assemble into multicellular communities. Acts with Hpr as a corepressor of epr expression. Also negatively regulates transcription of the lutABC operon, which is required for lactate utilization. Repressor activity is regulated by SinI.[1] [2] [3] [4]
About this Structure
3zkc is a 4 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full crystallographic information is available from OCA.
Reference
- ↑ Gaur NK, Oppenheim J, Smith I. The Bacillus subtilis sin gene, a regulator of alternate developmental processes, codes for a DNA-binding protein. J Bacteriol. 1991 Jan;173(2):678-86. PMID:1898931
- ↑ Mandic-Mulec I, Doukhan L, Smith I. The Bacillus subtilis SinR protein is a repressor of the key sporulation gene spo0A. J Bacteriol. 1995 Aug;177(16):4619-27. PMID:7642487
- ↑ Kearns DB, Chu F, Branda SS, Kolter R, Losick R. A master regulator for biofilm formation by Bacillus subtilis. Mol Microbiol. 2005 Feb;55(3):739-49. PMID:15661000 doi:10.1111/j.1365-2958.2004.04440.x
- ↑ Kodgire P, Dixit M, Rao KK. ScoC and SinR negatively regulate epr by corepression in Bacillus subtilis. J Bacteriol. 2006 Sep;188(17):6425-8. PMID:16923912 doi:10.1128/JB.00427-06
