Structural highlights
Function
PLAS1_POPNI Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Plastocyanin is an electron-transfer protein which has been largely used for biophysical studies as well as for protein-engineering experiments. A surface disulfide bridge has been engineered in poplar plastocyanin to allow protein chemisorption on gold substrates. The mutated plastocyanin crystal structure has been studied at 1.6 A resolution (R factor = 0.145, R(free) = 0.205) to characterize the effects of the engineered disulfide on the overall protein structure and on the Cu-coordination sphere in view of biophysical applications. The new orthorhombic crystal form isolated for the mutated plastocyanin displays two protein molecules per asymmetric unit.
The 1.6 A resolution crystal structure of a mutant plastocyanin bearing a 21-25 engineered disulfide bridge.,Milani M, Andolfi L, Cannistraro S, Verbeet MP, Bolognesi M Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1735-8. Epub 2001, Oct 25. PMID:11679761[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Milani M, Andolfi L, Cannistraro S, Verbeet MP, Bolognesi M. The 1.6 A resolution crystal structure of a mutant plastocyanin bearing a 21-25 engineered disulfide bridge. Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1735-8. Epub 2001, Oct 25. PMID:11679761
