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Crystal-structure of azotobacter cytochrome-c5 at 2.5-a resolution

Academic Article
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Overview

authors

  • Carter, D. C.
  • Melis, K. A.
  • Odonnell, S. E.
  • Burgess, B. K.
  • Furey, W. F.
  • Wang, B. C.
  • Stout, C. David

publication date

  • 1985

journal

  • Journal of Molecular Biology  Journal

abstract

  • The crystal structure of cytochrome c5 from Azotobacter vinelandii has been solved and refined to an R value of 0.29 at 2.5 A resolution. The structure of the oxidized protein was solved using a monoclinic crystal form. The structure was solved by multiple isomorphous replacements, re-fit to a solvent-leveled multiple isomorphous replacement map, and refined by restrained least squares. The structure reveals monomers associated about the crystallographic 2-fold axis by hydrophobic contacts at the "exposed heme edge". The overall conformation for the monomer is similar to that of Pseudomonas aeruginosa cytochrome c551. However, relative to a common heme conformation, c5 and c551 differ by an average of 6.8 A over 82 alpha-carbon positions and the propionates of c5 are much more exposed to solvent. The shortest heme--heme contact at the "dimer" interface is 6.3 A (Fe to Fe 16.4 A). Alignment of c5 and c551 shows that the two cytochromes, in spite of sequence differences, have remarkably similar charge distributions. A disulfide stacks on a tyrosine between the N- and C-terminal helices.

subject areas

  • Amino Acid Sequence
  • Azotobacter
  • Crystallography
  • Cytochrome c Group
  • Pseudomonas
  • Pseudomonas aeruginosa
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/0022-2836(85)90380-8

PubMed ID

  • 2993632
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Additional Document Info

start page

  • 279

end page

  • 295

volume

  • 184

issue

  • 2

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