Open AccessExpression, crystallization and preliminary crystallographic analysis of SufE (XAC2355) from Xanthomonas axonopodis pv. citri
Author(s) -
Guzzo Cristiane R.,
Silva Lucicleide R.,
GalvãoBotton Leonor M. P.,
Barbosa João A. R. G.,
Farah Chuck S.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106004945
Subject(s) - crystallization , crystallography , xanthomonas , biology , chemistry , genetics , bacteria , organic chemistry
Xanthomonas axonopodis pv. citri ( Xac ) SufE (XAC2355) is a member of a family of bacterial proteins that are conserved in several pathogens and phytopathogens. The Escherichia coli suf operon is involved in iron–sulfur cluster biosynthesis under iron‐limitation and stress conditions. It has recently been demonstrated that SufE and SufS form a novel two‐component cysteine desulfarase in which SufS catalyses the conversion of l ‐cysteine to l ‐alanine, forming a protein‐bound persulfide intermediate. The S atom is then transferred to SufE, from which it is subsequently transferred to target molecules or reduced to sulfide in solution. Here, the cloning, expression, crystallization and phase determination of Xac SufE crystals are described. Recombinant SufE was crystallized in space group P 2 1 2 1 2 1 and diffracted to 1.9 Å resolution at a synchrotron source. The unit‐cell parameters are a = 45.837, b = 58.507, c = 98.951 Å, α = β = γ = 90°. The calculated Matthews coefficient indicated the presence of two molecules in the asymmetric unit. Phasing was performed by molecular‐replacement using E. coli SufE as a model (PDB code 1mzg ) and an interpretable map was obtained.