2rs4

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[[Image:2rs4.png|left|200px]]
 
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{{STRUCTURE_2rs4| PDB=2rs4 | SCENE= }}
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===NMR strucure of stereo-array isotope labelled (SAIL) peptidyl-prolyl cis-trans isomerase from E. coli (EPPIb)===
===NMR strucure of stereo-array isotope labelled (SAIL) peptidyl-prolyl cis-trans isomerase from E. coli (EPPIb)===
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{{ABSTRACT_PUBMED_21955241}}
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==Function==
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[[http://www.uniprot.org/uniprot/PPIB_ECOLI PPIB_ECOLI]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
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(as it appears on PubMed at http://www.pubmed.gov), where 21955241 is the PubMed ID number.
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{{ABSTRACT_PUBMED_21955241}}
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==About this Structure==
==About this Structure==
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[[2rs4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RS4 OCA].
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[[2rs4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RS4 OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:021955241</ref><references group="xtra"/>
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<ref group="xtra">PMID:021955241</ref><references group="xtra"/><references/>
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[[Category: Escherichia coli]]
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[[Category: Escherichia coli k-12]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Jee, J.]]
[[Category: Jee, J.]]

Revision as of 18:18, 19 June 2013

Template:STRUCTURE 2rs4

Contents

NMR strucure of stereo-array isotope labelled (SAIL) peptidyl-prolyl cis-trans isomerase from E. coli (EPPIb)

Template:ABSTRACT PUBMED 21955241

Function

[PPIB_ECOLI] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

About this Structure

2rs4 is a 1 chain structure with sequence from Escherichia coli k-12. Full experimental information is available from OCA.

Reference

  • Takeda M, Jee J, Ono AM, Terauchi T, Kainosho M. Hydrogen Exchange Study on the Hydroxyl Groups of Serine and Threonine Residues in Proteins and Structure Refinement Using NOE Restraints with Polar Side-Chain Groups. J Am Chem Soc. 2011 Oct 10. PMID:21955241 doi:10.1021/ja206799v

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