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

Academic Article
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Overview

authors

  • Moore, J. M.
  • Case, David A.
  • Chazin, Walter J.
  • Gippert, Garry
  • Havel, T. F.
  • Powls, R.
  • Wright, Peter

publication date

  • April 1988

journal

  • Science  Journal

abstract

  • 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.

subject areas

  • Calorimetry
  • Chlorophyta
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Plant Proteins
  • Plastocyanin
  • Protein Conformation
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Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.3353725

PubMed ID

  • 3353725
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Additional Document Info

start page

  • 314

end page

  • 317

volume

  • 240

issue

  • 4850

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