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• W2021122243 abstract "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′. The structure adopts a conserved β-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′ demonstrate the absolute requirement of residue C127 for noncovalent heme binding in vitro." @default.
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• W2021122243 date "2012-04-24" @default.
• W2021122243 modified "2023-10-17" @default.
• W2021122243 title "Solution NMR Structure, Backbone Dynamics, and Heme-Binding Properties of a Novel Cytochrome <i>c</i> Maturation Protein CcmE from <i>Desulfovibrio vulgaris</i>" @default.
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• W2021122243 doi "https://doi.org/10.1021/bi300457b" @default.
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