1ist

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Crystal structure of yeast cyclophilin A, CPR1Crystal structure of yeast cyclophilin A, CPR1

Structural highlights

1ist is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CYPH_YEAST PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in histone deacetylase complexes, suggesting a function in chromatin. Imports fructose-1,6-bisphosphatase (FBPase) into the intermediate vacuole import and degradation (Vid) vesicles.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. Brown CR, Cui DY, Hung GG, Chiang HL. Cyclophilin A mediates Vid22p function in the import of fructose-1,6-bisphosphatase into Vid vesicles. J Biol Chem. 2001 Dec 21;276(51):48017-26. Epub 2001 Oct 18. PMID:11641409 doi:http://dx.doi.org/10.1074/jbc.M109222200

1ist, resolution 1.90Å

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OCA