3gdv: Difference between revisions

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===Crystal structure of DegS H198P/D320A mutant modified by DFP and in complex with YQF peptide===
===Crystal structure of DegS H198P/D320A mutant modified by DFP and in complex with YQF peptide===


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{{ABSTRACT_PUBMED_19836340}}


==About this Structure==
==About this Structure==
3GDV is a 6 chains structure of sequences 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=3GDV OCA].  
3GDV is a 6 chains structure with sequences 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=3GDV OCA].  
 
==Reference==
<ref group="xtra">PMID:19836340</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Grant, R A.]]
[[Category: Grant, R A.]]
Line 21: Line 30:
[[Category: Htra]]
[[Category: Htra]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Hydrolase/hydrolase activator complex]]
[[Category: Hydrolase-hydrolase activator complex]]
[[Category: Pdz omp]]
[[Category: Pdz omp]]
[[Category: Periplasm]]
[[Category: Protease]]
[[Category: Protease]]
[[Category: Serine protease]]
[[Category: Serine protease]]
[[Category: Stress-sensor]]
[[Category: Stress-sensor]]


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Revision as of 07:12, 25 August 2010

File:3gdv.png

Template:STRUCTURE 3gdv

Crystal structure of DegS H198P/D320A mutant modified by DFP and in complex with YQF peptideCrystal structure of DegS H198P/D320A mutant modified by DFP and in complex with YQF peptide

Template:ABSTRACT PUBMED 19836340

About this StructureAbout this Structure

3GDV is a 6 chains structure with sequences from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Sohn J, Grant RA, Sauer RT. OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism. Structure. 2009 Oct 14;17(10):1411-21. PMID:19836340 doi:10.1016/j.str.2009.07.017

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