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.
Original language | English (US) |
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Pages (from-to) | 3705-3707 |
Number of pages | 3 |
Journal | Biochemistry |
Volume | 51 |
Issue number | 18 |
DOIs | |
State | Published - May 8 2012 |
Externally published | Yes |