ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
A preliminary crystallographic study of recombinant NicX, an Fe(2+)-dependent 2,5-dihydroxypyridine dioxygenase from Pseudomonas putida KT2440.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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1 citing paper in PubMed, 4 citations in OpenAlex.
- Iron(II)-dependent dioxygenase and N-formylamide deformylase catalyze the reactions from 5-hydroxy-2-pyridone to maleamate.Scientific reports · 2013Article
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5 authors at 2 institutions in 1 country.
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Abstract
NicX from Pseudomonas putida KT2440 is an Fe(2+)-dependent dioxygenase that is involved in the aerobic degradation of nicotinic acid. The enzyme converts 2,5-dihydroxypyridine to N-formylmaleamic acid when overexpressed in Escherichia coli. Biophysical characterization of NicX by analytical gel-filtration chromatography revealed that it behaves as an oligomeric assembly in solution, with an apparent molecular weight that is consistent with a hexameric species. NicX was crystallized by the hanging-drop vapour-diffusion method at 291 K. Diffraction data were collected to a resolution of 2.0 A at the ESRF. The crystals most probably belong to the orthorhombic space group C222 or C222(1). The estimated Matthews coefficient was 2.4 A(3) Da(-1), corresponding to 50% solvent content, which is consistent with the presence of three protein molecules in the asymmetric unit. Analysis of the crystal data together with chromatographic results supports NicX being a hexameric assembly composed of two cyclic trimers. Currently, crystallization of recombinant selenomethionine-containing NicX is in progress.
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