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Science 15 April 1988:
Vol. 240. no. 4850, pp. 314 - 317
DOI: 10.1126/science.3353725

Articles

Science, Vol 240, Issue 4850, 314-317
Copyright © 1988 by American Association for the Advancement of Science


articles

Three-dimensional solution structure of plastocyanin from the green alga Scenedesmus obliquus

JM Moore, DA Case, WJ Chazin, GP Gippert, TF Havel, R Powls, and PE Wright

Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037.

The solution conformation of plastocyanin from the green alga Scenedesmus obliquus has been determined from distance and dihedral angle constraints derived by nuclear magnetic resonance (NMR) spectroscopy. Structures were generated with distance geometry and restrained molecular dynamics calculations. A novel molecular replacement method was also used with the same NMR constraints to generate solution structures of S. obliquus plastocyanin from the x-ray structure of the homologous poplar protein. Scenedesmus obliquus plastocyanin in solution adopts a beta-barrel structure. The backbone conformation is well defined and is similar overall to that of poplar plastocyanin in the crystalline state. The distinctive acidic region of the higher plant plastocyanins, which functions as a binding site for electron transfer proteins and inorganic complexes, differs in both shape and charge in S. obliquus plastocyanin.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
The Structure and Unusual pH Dependence of Plastocyanin from the Fern Dryopteris crassirhizoma. THE PROTONATION OF AN ACTIVE SITE HISTIDINE IS HINDERED BY {pi}-{pi} INTERACTIONS.
T. Kohzuma, T. Inoue, F. Yoshizaki, Y. Sasakawa, K. Onodera, S. Nagatomo, T. Kitagawa, S. Uzawa, Y. Isobe, Y. Sugimura, et al. (1999)
J. Biol. Chem. 274, 11817-11823
   Abstract »    Full Text »    PDF »
Novel Insight into the Copper-Ligand Geometry in the Crystal Structure of Ulva pertusa Plastocyanin at 1.6-A Resolution. STRUCTURAL BASIS FOR REGULATION OF THE COPPER SITE BY RESIDUE 88.
N. Shibata, T. Inoue, C. Nagano, N. Nishio, T. Kohzuma, K. Onodera, F. Yoshizaki, Y. Sugimura, and Y. Kai (1999)
J. Biol. Chem. 274, 4225-4230
   Abstract »    Full Text »    PDF »



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