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1YLB

NMR solution structure of the reduced spinach plastocyanin

Summary for 1YLB
Entry DOI10.2210/pdb1ylb/pdb
DescriptorPlastocyanin, chloroplast, COPPER (I) ION (2 entities in total)
Functional Keywordsplastocyanin, copper(+)-containing, electron-transfer, spinach, photosynthesis, blue-copper protein, electron transport
Biological sourceSpinacia oleracea (spinach)
Cellular locationPlastid, chloroplast thylakoid membrane; Peripheral membrane protein; Lumenal side: P00289
Total number of polymer chains1
Total formula weight10484.10
Authors
Musiani, F.,Dikiy, A.,Semenov, A.Y.,Ciurli, S. (deposition date: 2005-01-19, release date: 2005-04-05, Last modification date: 2024-05-22)
Primary citationMusiani, F.,Dikiy, A.,Semenov, A.Y.,Ciurli, S.
Structure of the Intermolecular Complex between Plastocyanin and Cytochrome f from Spinach.
J.Biol.Chem., 280:18833-18841, 2005
Cited by
PubMed Abstract: In oxygenic photosynthesis, plastocyanin shuttles electrons between the membrane-bound complexes cytochrome b6f and photosystem I. The homologous complex between cytochrome f and plastocyanin, both from spinach, is the object of this study. The solution structure of the reduced spinach plastocyanin was determined using high field NMR spectroscopy, whereas the model structure of oxidized cytochrome f was obtained by homology modeling calculations and molecular dynamics. The model structure of the intermolecular complex was calculated using the program AUTODOCK, taking into account biological information obtained from mutagenesis experiments. The best electron transfer pathway from the heme group of cytochrome f to the copper ion of plastocyanin was calculated using the program HARLEM, obtaining a coupling decay value of 1.8 x 10(-4). Possible mechanisms of interaction and electron transfer between plastocyanin and cytochrome f were discussed considering the possible formation of a supercomplex that associates one cytochrome b6f, one photosystem I, and one plastocyanin.
PubMed: 15691836
DOI: 10.1074/jbc.M412760200
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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