Purification, crystallization and preliminary crystallographic analysis of a dissimilatory DsrAB sulfite reductase in complex with DsrC.
Dissimilatory sulfite reductase (dSiR, DsrAB) is a key protein in dissimilatory sulfur metabolism, one of the earliest types of energy metabolism to be traced on earth. dSirs are large oligomeric proteins around 200kDa forming an alpha(2)beta(2) arrangement and including a unique siroheme-[4Fe-4S] coupled cofactor. Here, we report the purification, crystallization and preliminary X-ray diffraction analysis of dSir isolated from Desulfovibrio vulgaris Hildenborough, also known as desulfoviridin. In this enzyme the DsrAB protein is associated with DsrC, a protein of unknown function that is believed to play an important role in the sulfite reduction. Crystals belong to the monoclinic space group P2(1) with unit-cell parameters a=122.7, b=119.4 and c=146.7A and beta =110.0 degrees , and diffract X-rays to 2.8A on a synchrotron source.
Oliveira
Tânia F
TF
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa (ITQB-UNL), Av. da República-EAN, 2780-157 Oeiras, Portugal.
Vonrhein
Clemens
C
Matias
Pedro M
PM
Venceslau
Sofia S
SS
Pereira
Inês A C
IA
Archer
Margarida
M
D003460:Crystallization; D018360:Crystallography, X-Ray; D016969:Desulfovibrio vulgaris / Q000201:enzymology*; D050885:Hydrogensulfite Reductase / Q000737:chemistry* / Q000302:isolation & purification; D013447:Sulfites / Q000378:metabolism; D013455:Sulfur / Q000378:metabolism
D013447:Sulfites; D013455:Sulfur; D050885:Hydrogensulfite Reductase