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Publication Abstract from PubMed

The crystal structure of the 'blue' copper protein plastocyanin from the cyanobacterium Phormidium laminosum has been solved and refined using 2.8 A X--ray data. P. laminosum plastocyanin crystallizes in space group P43212 with unit-cell dimensions a = 86.57, c = 91.47 A and with three protein molecules per asymmetric unit. The final residual R is 19.9%. The structure was solved using molecular replacement with a search model based on the crystal structure of a close homologue, Anabaena variabilis plastocyanin (66% sequence identity). The molecule of P. laminosum plastocyanin has 105 amino-acid residues. The single Cu atom is coordinated by the same residues - two histidines, a cysteine and a methionine - as in other plastocyanins. In the crystal structure, the three molecules of the asymmetric unit are related by a non-crystallographic threefold axis. A Zn atom lies between each pair of neighbouring molecules in this ensemble, being coordinated by a surface histidine residue of one molecule and by two aspartates of the other.

The structure of plastocyanin from the cyanobacterium Phormidium laminosum.,Bond CS, Bendall DS, Freeman HC, Guss JM, Howe CJ, Wagner MJ, Wilce MC Acta Crystallogr D Biol Crystallogr. 1999 Feb;55(Pt 2):414-21. PMID:10089349^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.