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Refinement of the fe-7 ferredoxin from azotobacter-vinelandii at 1.9-a resolution

Academic Article
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Overview

authors

  • Stout, C. David

publication date

  • February 1989

journal

  • Journal of Molecular Biology  Journal

abstract

  • The recently redetermined structure of the 7 Fe ferredoxin from Azotobacter vinelandii has been refined against a new 1.9 A data set. The crystallographic R-factor is 0.215 for all 9586 observed reflections 8.0 to 1.9 A. The model contains 106 amino acid residues, two Fe-S clusters and 21 water molecules. The root-mean-square deviations from ideality of bonds and angles are 0.014 A and 3.3 degrees, respectively. The refinement confirms the presence of two free cysteines: the thiol of C11 is in association with the side-chain of K100; the thiol of C24 is 3.35 A from inorganic sulfur of the [4 Fe-4 S] cluster. The refinement confirms a [3 Fe-4 S] model for the 3 Fe cluster. The two Fe-S clusters have similar bond distances and angles. The structure of the protein for residues 1 to 57 superposes within 0.85 A on residues 1 to 53 of the 8 Fe ferredoxin structure for main-chain N, CA and C atoms, if residues 9, 10, 29 and 30 of 7 Fe ferredoxin are omitted. These residues are part of two loops in contact with residues of the extended C-terminal chain of 7 Fe ferredoxin.

subject areas

  • Amino Acids
  • Azotobacter
  • Bacterial Proteins
  • Ferredoxins
  • Hydrogen Bonding
  • Models, Molecular
  • Protein Conformation
  • X-Ray Diffraction
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/0022-2836(89)90225-8

PubMed ID

  • 2926817
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Additional Document Info

start page

  • 545

end page

  • 555

volume

  • 205

issue

  • 3

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