Structure of cytochrome c2 from Rhodospirillum centenum

Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1498-505. doi: 10.1107/s0907444901010423. Epub 2001 Oct 25.

Abstract

Cytochrome c(2) from the purple photosynthetic bacterium Rhodospirillum centenum has been crystallized by the sitting-drop vapour-diffusion method. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 29.7, b = 59.9, c = 65.4 A, and diffract to a resolution limit of 1.7 A. The Fe-atom position was determined from its anomalous scattering contribution and a molecular-replacement solution was calculated. The correctness of the solution was confirmed by parallel isomorphous replacement studies. The resulting model has a type I cytochrome fold with two features, an extended alpha-helix and a surface-charge distribution, that are distinctive to this protein. The implications of these structural features for the ability of the cytochrome to serve as an electron carrier are discussed.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Cytochrome c Group / chemistry*
  • Cytochromes c2
  • Models, Molecular
  • Protein Conformation
  • Rhodospirillum / enzymology*

Substances

  • Cytochrome c Group
  • Cytochromes c2

Associated data

  • PDB/1JDL