Expression, crystallization and preliminary crystallographic studies of a novel bifunctional N-acetylglutamate synthase/kinase from Xanthomonas campestris homologous to vertebrate N-acetylglutamate synthase.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 62(Pt 12): 1218-22, 2006 Dec 01.
Article
en En
| MEDLINE
| ID: mdl-17142901
ABSTRACT
A novel N-acetylglutamate synthase/kinase bifunctional enzyme of arginine biosynthesis that was homologous to vertebrate N-acetylglutamate synthases was identified in Xanthomonas campestris. The protein was overexpressed, purified and crystallized. The crystals belong to the hexagonal space group P6(2)22, with unit-cell parameters a = b = 134.60, c = 192.11 A, and diffract to about 3.0 A resolution. Selenomethionine-substituted recombinant protein was produced and selenomethionine substitution was verified by mass spectroscopy. Multiple anomalous dispersion (MAD) data were collected at three wavelengths at SER-CAT, Advanced Photon Source, Argonne National Laboratory. Structure determination is under way using the MAD phasing method.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Xanthomonas campestris
/
Fosfotransferasas (aceptor de Grupo Carboxilo)
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N-Acetiltransferasa de Aminoácidos
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Complejos Multienzimáticos
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Año:
2006
Tipo del documento:
Article
País de afiliación:
Estados Unidos