Solution NMR Structure, Backbone Dynamics, and Heme-Binding Properties of a Novel Cytochrome c Maturation Protein CcmE from Desulfovibrio vulgaris

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• 作者：James M. Aramini ; Keith Hamilton ; Paolo Rossi ; Asli Ertekin ; Hsiau-Wei Lee ; Alexander Lemak ; Huang Wang ; Rong Xiao ; Thomas B. Acton ; John K. Everett ; Gaetano T. Montelione
• 刊名：Biochemistry
• 出版年：2012
• 出版时间：May 8, 2012
• 年：2012
• 卷：51
• 期：18
• 页码：3705-3707
• 全文大小：227K
• 年卷期：v.51,no.18(May 8, 2012)
• ISSN：1520-4995

文摘

Cytochrome c maturation protein E, CcmE, plays an integral role in the transfer of heme to apocytochrome c in many prokaryotes and some mitochondria. A novel subclass featuring a heme-binding cysteine has been identified in archaea and some bacteria. Here we describe the solution NMR structure, backbone dynamics, and heme binding properties of the soluble C-terminal domain of Desulfovibrio vulgaris CcmE, dvCcmE鈥? The structure adopts a conserved 尾-barrel OB fold followed by an unstructured C-terminal tail encompassing the CxxxY heme-binding motif. Heme binding analyses of wild-type and mutant dvCcmE鈥?demonstrate the absolute requirement of residue C127 for noncovalent heme binding in vitro.