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

ASJC Scopus subject areas

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

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