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

Swairjo MA, Reddy RR, Lee B, Van Lanen SG, Brown S, de Crecy-Lagard V, Iwata-Reuyl D, Schimmel P

Published 2005-10-01 in Acta Crystallogr Sect F Struct Biol Cryst Commun volume 61 .

Pubmed ID: 16511203
DOI identifier: -

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 A. 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 A resolution.

This publication refers to following proteins:

Last modification of this entry: Sept. 6, 2012