2v42
From Proteopedia
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==Overview== | ==Overview== | ||
| - | An elegant network of signal transduction has evolved in the bacterial | + | An elegant network of signal transduction has evolved in the bacterial cell envelope to respond to environmental stress. It is initiated by sensing unfavourable and harmful changes in the periplasm. The stress signal is then transmitted by a controlled degradation of the transmembrane anti-sigma-factor RseA that leads to the activation of the alternative sigma factor sigma(E). The periplasmic protein RseB exerts a crucial role in modulating the stability of RseA. RseB from Escherichia coli has been crystallized and crystal structures were determined at 2.4 A and at 2.8 A resolution. The protein forms a homodimer, with the monomer composed of two domains. The large domain resembles an unclosed beta-barrel that is structurally remarkably similar to a protein family capable of binding the lipid anchor of lipoproteins. The small C-terminal domain, connected to the large domain by a partially unstructured loop, is responsible for interaction with RseA. On the basis of the structure of RseB, we suggest that it acts as a sensor of periplasmic stress with a dual functionality: it detects mislocalized lipoproteins and propagates the signal to induce the sigma(E)-response. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | The | + | The structure of RseB: a sensor in periplasmic stress response of E. coli., Wollmann P, Zeth K, J Mol Biol. 2007 Sep 28;372(4):927-41. Epub 2007 Jun 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17692869 17692869] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: sensor for periplasmic stress]] | [[Category: sensor for periplasmic stress]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:53:07 2008'' |
Revision as of 16:53, 21 February 2008
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CRYSTAL STRUCTURE OF RSEB: A SENSOR FOR PERIPLASMIC STRESS RESPONSE IN E. COLI
Overview
An elegant network of signal transduction has evolved in the bacterial cell envelope to respond to environmental stress. It is initiated by sensing unfavourable and harmful changes in the periplasm. The stress signal is then transmitted by a controlled degradation of the transmembrane anti-sigma-factor RseA that leads to the activation of the alternative sigma factor sigma(E). The periplasmic protein RseB exerts a crucial role in modulating the stability of RseA. RseB from Escherichia coli has been crystallized and crystal structures were determined at 2.4 A and at 2.8 A resolution. The protein forms a homodimer, with the monomer composed of two domains. The large domain resembles an unclosed beta-barrel that is structurally remarkably similar to a protein family capable of binding the lipid anchor of lipoproteins. The small C-terminal domain, connected to the large domain by a partially unstructured loop, is responsible for interaction with RseA. On the basis of the structure of RseB, we suggest that it acts as a sensor of periplasmic stress with a dual functionality: it detects mislocalized lipoproteins and propagates the signal to induce the sigma(E)-response.
About this Structure
2V42 is a Single protein structure of sequence from Escherichia coli with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
The structure of RseB: a sensor in periplasmic stress response of E. coli., Wollmann P, Zeth K, J Mol Biol. 2007 Sep 28;372(4):927-41. Epub 2007 Jun 19. PMID:17692869
Page seeded by OCA on Thu Feb 21 18:53:07 2008
