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Structural highlights

Function

FKB13_ARATH PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Responsive of the major PPIase activity in the chloroplast thylakoid lumen. Regulates the accumulation of Rieske protein, an essential component of the photosynthetic electron transport chain.^{[1] [2] [3]}

Evolutionary Conservation

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

See Also

• FKBP 3D structures

References

1. ↑ Shapiguzov A, Edvardsson A, Vener AV. Profound redox sensitivity of peptidyl-prolyl isomerase activity in Arabidopsis thylakoid lumen. FEBS Lett. 2006 Jun 26;580(15):3671-6. PMID:16765949 doi:http://dx.doi.org/10.1016/j.febslet.2006.05.054
2. ↑ Edvardsson A, Shapiguzov A, Petersson UA, Schroder WP, Vener AV. Immunophilin AtFKBP13 sustains all peptidyl-prolyl isomerase activity in the thylakoid lumen from Arabidopsis thaliana deficient in AtCYP20-2. Biochemistry. 2007 Aug 21;46(33):9432-42. Epub 2007 Jul 27. PMID:17655280 doi:http://dx.doi.org/10.1021/bi700426q
3. ↑ Ingelsson B, Shapiguzov A, Kieselbach T, Vener AV. Peptidyl-prolyl isomerase activity in chloroplast thylakoid lumen is a dispensable function of immunophilins in Arabidopsis thaliana. Plant Cell Physiol. 2009 Oct;50(10):1801-14. doi: 10.1093/pcp/pcp122. Epub 2009, Aug 28. PMID:19717822 doi:http://dx.doi.org/10.1093/pcp/pcp122