Solution NMR structure, backbone dynamics, and heme-binding properties of a novel cytochrome c maturation protein CcmE from Desulfovibrio vulgaris

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

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

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 languageEnglish (US)
Pages (from-to)3705-3707
Number of pages3
JournalBiochemistry
Volume51
Issue number18
DOIs
StatePublished - May 8 2012

Fingerprint Dive into the research topics of 'Solution NMR structure, backbone dynamics, and heme-binding properties of a novel cytochrome c maturation protein CcmE from Desulfovibrio vulgaris'. Together they form a unique fingerprint.

Cite this