2pv2: Difference between revisions

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==About this Structure==
==About this Structure==
2PV2 is a [[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=2PV2 OCA].  
2PV2 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=2PV2 OCA].  


==Reference==
==Reference==
The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues., Xu X, Wang S, Hu YX, McKay DB, J Mol Biol. 2007 Oct 19;373(2):367-81. Epub 2007 Aug 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17825319 17825319]
<ref group="xtra">PMID:17825319</ref><ref group="xtra">PMID:12429090</ref><references group="xtra"/>
 
Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins., Bitto E, McKay DB, Structure. 2002 Nov;10(11):1489-98. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12429090 12429090]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Single protein]]
[[Category: McKay, D B.]]
[[Category: McKay, D B.]]
[[Category: Xu, X.]]
[[Category: Xu, X.]]
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[[Category: Survival protein some]]
[[Category: Survival protein some]]


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Revision as of 09:22, 17 February 2009

File:2pv2.png

Template:STRUCTURE 2pv2

Crystallographic Structure of SurA first peptidyl-prolyl isomerase domain complexed with peptide NFTLKFWDIFRKCrystallographic Structure of SurA first peptidyl-prolyl isomerase domain complexed with peptide NFTLKFWDIFRK

Template:ABSTRACT PUBMED 17825319

About this StructureAbout this Structure

2PV2 is a 6 chains structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1][xtra 2]

  1. Xu X, Wang S, Hu YX, McKay DB. The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues. J Mol Biol. 2007 Oct 19;373(2):367-81. Epub 2007 Aug 15. PMID:17825319 doi:10.1016/j.jmb.2007.07.069
  2. Bitto E, McKay DB. Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins. Structure. 2002 Nov;10(11):1489-98. PMID:12429090

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