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Crystallization and preliminary X-ray characterization of the nitrile reductase QueF: A queuosine-biosynthesis enzyme

  • Manal A. Swairjo
  • , Robert R. Reddy
  • , Bobby Lee
  • , Steven G. Van Lanen
  • , Shannon Brown
  • , Valérie De Crécy-Lagard
  • , Dirk Iwata-Reuyl
  • , Paul Schimmel

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

QueF (MW = 19.4 kDa) is a recently characterized nitrile oxidoreductase which catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine, a late step in the biosynthesis of the modified tRNA nucleoside queuosine. Initial crystals of homododecameric Bacillus subtilis QueF diffracted poorly to 8.0 Å. A three-dimensional model based on homology with the tunnel-fold enzyme GTP cyclohydrolase I suggested catalysis at intersubunit interfaces and a potential role for substrate binding in quaternary structure stabilization. Guided by this insight, a second crystal form was grown that was strictly dependent on the presence of preQ0. This crystal form diffracted to 2.25 Å resolution.

Original languageEnglish
Pages (from-to)945-948
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume61
Issue number10
DOIs
StatePublished - 2005

Funding

FundersFunder number
National Institute of General Medical SciencesR37GM015539

    ASJC Scopus subject areas

    • Biophysics
    • Structural Biology
    • Biochemistry
    • Genetics
    • Condensed Matter Physics

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