Crystallization and preliminary X-ray characterization of the nitrile reductase QueF: a queuosine-biosynthesis enzyme
| Autor: | Paul Schimmel, Bobby W.K. Lee, Manal A. Swairjo, Shannon Brown, Steven G. Van Lanen, Valérie de Crécy-Lagard, Dirk Iwata-Reuyl, Robert Reddy |
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| Rok vydání: | 2005 |
| Předmět: |
Models
Molecular Guanine Nitrile Protein Conformation Stereochemistry GTP cyclohydrolase I Biophysics Queuosine Pyrimidinones Reductase Crystallography X-Ray Biochemistry Catalysis chemistry.chemical_compound RNA Transfer X-Ray Diffraction Structural Biology Oxidoreductase Nucleoside Q Genetics Protein Isoforms Pyrroles RNA Processing Post-Transcriptional GTP Cyclohydrolase chemistry.chemical_classification biology Computational Biology Substrate (chemistry) Condensed Matter Physics Protein Structure Tertiary Crystallography Models Chemical chemistry Crystallization Communications biology.protein Protein quaternary structure Crystallization Oxidoreductases NADP Bacillus subtilis |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61:945-948 |
| ISSN: | 1744-3091 |
| DOI: | 10.1107/s1744309105029246 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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