2pv2: Difference between revisions
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[[Image:2pv2.png|left|200px]] | [[Image:2pv2.png|left|200px]] | ||
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==About this Structure== | ==About this Structure== | ||
[[2pv2]] 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=2PV2 OCA]. | |||
==Reference== | ==Reference== | ||
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[[Category: Peptidyl-prolyl cis-trans isomerase domain]] | [[Category: Peptidyl-prolyl cis-trans isomerase domain]] | ||
[[Category: Survival protein some]] | [[Category: Survival protein some]] | ||
Revision as of 23:59, 14 March 2011
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 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ 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
- ↑ 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