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. 1998 Oct;7(10):2099–2105. doi: 10.1002/pro.5560071006

Crystal structure of spinach plastocyanin at 1.7 A resolution.

Y Xue 1, M Okvist 1, O Hansson 1, S Young 1
PMCID: PMC2143848  PMID: 9792096

Abstract

The crystal structure of plastocyanin from spinach has been determined using molecular replacement, with the structure of plastocyanin from poplar as a search model. Successful crystallization was facilitated by site-directed mutagenesis in which residue Gly8 was substituted with Asp. The region around residue 8 was believed to be too mobile for the wild-type protein to form crystals despite extensive screening. The current structure represents the oxidized plastocyanin, copper (II), at low pH (approximately 4.4). In contrast to the similarity in the core region as compared to its poplar counterpart, the structure shows some significant differences in loop regions. The most notable is the large shift of the 59-61 loop where the largest shift is 3.0 A for the C(alpha) atom of Glu59. This results in different patterns of electrostatic potential around the acidic patches for the two proteins.

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Selected References

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