Purification, crystallization and preliminary crystallographic analysis of a dissimilatory DsrAB sulfite reductase in complex with DsrC

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• 作者：Tâ ; nia F. Oliveira ; Clemens Vonrhein ; Pedro M. Matias ; Sofia S. Venceslau ; Inê ; s A.C. Pereira ; Margarida Archer
• 关键词：Crystallization ; MAD phasing ; Dissimilatory sulfite reductase ; DsrABC complex
• 刊名：Journal of Structural Biology
• 出版年：2008
• 出版时间：November 2008
• 年：2008
• 卷：164
• 期：2
• 页码：236-239
• 全文大小：188 K

文摘

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 200 kDa forming an α₂β₂ 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 P2₁ with unit-cell parameters a = 122.7, b = 119.4 and c = 146.7 Å and β =110.0°, and diffract X-rays to 2.8 Å on a synchrotron source.