1te0
From Proteopedia
(New page: 200px<br /><applet load="1te0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1te0, resolution 2.20Å" /> '''Structural analysis ...) |
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| - | [[Image:1te0.jpg|left|200px]]<br /><applet load="1te0" size=" | + | [[Image:1te0.jpg|left|200px]]<br /><applet load="1te0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1te0, resolution 2.20Å" /> | caption="1te0, resolution 2.20Å" /> | ||
'''Structural analysis of DegS, a stress sensor of the bacterial periplasm'''<br /> | '''Structural analysis of DegS, a stress sensor of the bacterial periplasm'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Regulated proteolysis is a key event in transmembrane signalling between | + | Regulated proteolysis is a key event in transmembrane signalling between intracellular compartments. In Escherichia coli the membrane-bound protease DegS has been identified as the periplasmic stress sensor for unfolded outer membrane proteins (OMPs). DegS inititates a proteolytic cascade resulting in the release of sigmaE the transcription factor of periplasmic genes. The crystal structure of DegS protease reported at 2.2 A resolution reveals a trimeric complex with the monomeric protease domain in an inhibited state followed by the inhibitory PDZ domain. Noteably, domain architecture and communication of DegS are remarkably to homologous proteins known to date. Here the domain interface is mechanically locked by three intradomain salt bridges. Co-crystallisation trials in the presence of a 10-residue activating peptide did not result in significant structural intradomain shifts nor distortions in the crystal packing. These observations imply a mode of activation indicative of peptide-induced structural shifts imposed to the protease domain rather than disturbing the PDZ-protease interface. |
==About this Structure== | ==About this Structure== | ||
| - | 1TE0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1TE0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TE0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Ravelli, R | + | [[Category: Ravelli, R B.G.]] |
[[Category: Zeth, K.]] | [[Category: Zeth, K.]] | ||
[[Category: alpha-beta protein]] | [[Category: alpha-beta protein]] | ||
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[[Category: x-ray structure]] | [[Category: x-ray structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:12:37 2008'' |
Revision as of 13:12, 21 February 2008
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Structural analysis of DegS, a stress sensor of the bacterial periplasm
Overview
Regulated proteolysis is a key event in transmembrane signalling between intracellular compartments. In Escherichia coli the membrane-bound protease DegS has been identified as the periplasmic stress sensor for unfolded outer membrane proteins (OMPs). DegS inititates a proteolytic cascade resulting in the release of sigmaE the transcription factor of periplasmic genes. The crystal structure of DegS protease reported at 2.2 A resolution reveals a trimeric complex with the monomeric protease domain in an inhibited state followed by the inhibitory PDZ domain. Noteably, domain architecture and communication of DegS are remarkably to homologous proteins known to date. Here the domain interface is mechanically locked by three intradomain salt bridges. Co-crystallisation trials in the presence of a 10-residue activating peptide did not result in significant structural intradomain shifts nor distortions in the crystal packing. These observations imply a mode of activation indicative of peptide-induced structural shifts imposed to the protease domain rather than disturbing the PDZ-protease interface.
About this Structure
1TE0 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural analysis of DegS, a stress sensor of the bacterial periplasm., Zeth K, FEBS Lett. 2004 Jul 2;569(1-3):351-8. PMID:15225661
Page seeded by OCA on Thu Feb 21 15:12:37 2008
