The 1.6 A resolution crystal structure of a mutant plastocyanin bearing a 21-25 engineered disulfide bridge.
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.
Milani
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M
Department of Physics-INFM, c/o Advanced Biotechnology Center-IST, University of Genova, Largo Rosanna Benzi 10, 16132 Genova, Italy.
Andolfi
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L
Cannistraro
S
S
Verbeet
M P
MP
Bolognesi
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M
D003460:Crystallization; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D009154:Mutation; D010970:Plastocyanin / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D015202:Protein Engineering; D011994:Recombinant Proteins / Q000737:chemistry; D014197:Trees / Q000737:chemistry*
D011994:Recombinant Proteins; D010970:Plastocyanin