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  • Title: The structure of plastocyanin from the cyanobacterium Phormidium laminosum.
    Author: Bond CS, Bendall DS, Freeman HC, Guss JM, Howe CJ, Wagner MJ, Wilce MC.
    Journal: Acta Crystallogr D Biol Crystallogr; 1999 Feb; 55(Pt 2):414-21. PubMed ID: 10089349.
    Abstract:
    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.
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