Compact reduced thioredoxin structure from the thermophilic bacteria Thermus thermophilus

Peter H. Rehse, Maki Kumei, Tahir H. Tahirov

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

The X-ray crystallographic structure of a thioredoxin from Thermus thermophilus was solved to 1.8 Å resolution by molecular replacement. The crystals' space group was C2 with cell dimensions of a= 40.91, b = 95.44, c = 56.68 Å, β =91.41°, with two molecules in the asymmetric unit. Unlike the reported thioredoxin structures, the biological unit of T. thermophilus thioredoxin is a dimer both, in solution and in the crystal. The fold conforms to the "thioredoxin fold" that is common over a class of nine protein families including thioredoxin; however, the folded portion of this protein is much more compact than other thioredoxins previously solved by X-ray crystallography being reduced by one α-helix and one β-strand. As with other thioredoxins, the active site is highly conserved even though the variation in sequence can be quite large. The T. thermophilus thioredoxin has some variability at the active site, especially compared with previously solved structures from bacterial sources.

Original languageEnglish (US)
Pages (from-to)1032-1037
Number of pages6
JournalProteins: Structure, Function and Genetics
Volume61
Issue number4
DOIs
StatePublished - Dec 1 2005

Keywords

  • Thioredoxin
  • X-ray crystal structure

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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