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A preliminary crystallographic study of recombinant NicX, a Fe2+-dependent 2,5-dihydroxypyridine dioxygenase from Pseudomonas putida KT2440

AutorJiménez, José Ignacio; Acebrón, Iván ; García, José Luis ; Díaz, Eduardo ; Mancheño, Jose M.
Palabras claveNicX
2,5-dihydroxypyridine dioxygenases
Pseudomonas putida KT2440
Fecha de publicaciónmay-2010
EditorInternational Union of Crystallography
CitaciónActa Crystallographica Section F: Structural Biology and Crystallization Communications 66(5):549-553(2010)
ResumenNicX from Pseudomonas putida KT2440 is an Fe2+-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 Å at the ESRF. The crystals most probably belong to the orthorhombic space group C222 or C2221. The estimated Matthews coefficient was 2.4 Å3 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
Descripción5 páginas, 4 figuras, 1 tabla -- PAGS nros. 549-553
Versión del editorhttp:dx.doi.org/0.1107/S174430911001119X
URIhttp://hdl.handle.net/10261/52555
DOI10.1107/S174430911001119X
ISSN1744-3091
E-ISSN1744-3091
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