Crystal structure of desulforedoxin from Desulfovibrio gigas determined at 1.8 Å resolution: a novel non-heme iron protein structure

Research output: Contribution to journalArticle

84 Citations (Scopus)

Abstract

The crystal structure of desulforedoxin from Desulfovibrio gigas, a new homo-dimeric (2×36 amino acids) non-heme iron protein, has been solved by the SIRAS method using the indium-substituted protein as the single derivative. The structure was refined to a crystallographic R-factor of 16.9% at 1.8 Å resolution. Native desulforedoxin crystals were grown from either PEG 4K or lithium sulfate, with cell constants a = b = 42.18 Å, c = 72.22 Å (for crystals grown from PEG 4K), and they belong to space group P3221. The indium-substituted protein crystallized isomorphously under the same conditions. The 2-fold symmetric dimer is firmly hydrogen bonded and folds as an incomplete β-barrel with the two iron centers placed on opposite poles of the molecule. Each iron atom is coordinated to four cysteinyl residues in a distorted tetrahedral arrangement. Both iron atoms are 16 Å apart but connected across the 2-fold axis by 14 covalent bonds along the polypeptide chain plus two hydrogen bonds. Desulforedoxin and rubredoxin share some structural features but show significant differences in terms of metal environment and water structure, which account for the known spectroscopic differences between rubredoxin and desulforedoxin.

Original languageEnglish
Pages (from-to)690-702
Number of pages13
JournalJournal of Molecular Biology
Volume251
Issue number5
DOIs
Publication statusPublished - 1 Aug 1995

Keywords

  • 3D structure
  • Crystallization
  • Desulforedoxin
  • Rubredoxin type proteins
  • Sulfate reducing bacteria
  • X-ray

Fingerprint Dive into the research topics of 'Crystal structure of desulforedoxin from Desulfovibrio gigas determined at 1.8 Å resolution: a novel non-heme iron protein structure'. Together they form a unique fingerprint.

  • Cite this