3gdu

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[[Image:3gdu.png|left|200px]]
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{{STRUCTURE_3gdu| PDB=3gdu | SCENE= }}
{{STRUCTURE_3gdu| PDB=3gdu | SCENE= }}
===Crystal structure of DegS H198P/D320A mutant modified by DFP and in complex with YRF peptide===
===Crystal structure of DegS H198P/D320A mutant modified by DFP and in complex with YRF peptide===
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{{ABSTRACT_PUBMED_19836340}}
==About this Structure==
==About this Structure==
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3GDU 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=3GDU OCA].
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[[3gdu]] is a 6 chain structure with 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=3GDU OCA].
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==Reference==
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<ref group="xtra">PMID:019836340</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Grant, R A.]]
[[Category: Grant, R A.]]
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[[Category: Htra]]
[[Category: Htra]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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[[Category: Hydrolase/hydrolase activator complex]]
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[[Category: Hydrolase-hydrolase activator complex]]
[[Category: Pdz omp]]
[[Category: Pdz omp]]
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[[Category: Periplasm]]
 
[[Category: Protease]]
[[Category: Protease]]
[[Category: Serine protease]]
[[Category: Serine protease]]
[[Category: Stress-sensor]]
[[Category: Stress-sensor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 4 20:31:33 2009''
 

Revision as of 14:30, 20 February 2013

Template:STRUCTURE 3gdu

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

Template:ABSTRACT PUBMED 19836340

About this Structure

3gdu is a 6 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  • 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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