The CcmC-CcmE interaction during cytochrome <i>c</i> maturation by System I is driven by protein-protein and not protein-heme contacts.

ABSTRACT: Cytochromes c are ubiquitous proteins, essential for life in most organisms. Their distinctive characteristic is the covalent attachment of heme to their polypeptide chain. This post-translational modification is performed by a dedicated protein system, which in many Gram-negative bacteria and plant mitochondria is a nine-protein apparatus (CcmA-I) called System I. Despite decades of study, mechanistic understanding of the protein-protein interactions in this highly complex maturation machinery is still lacking. Here, we focused on the interaction of CcmC, the protein that sources the heme cofactor, with CcmE, the pivotal component of System I responsible for the transfer of the heme to the apocytochrome. Using in silico analyses, we identified a putative interaction site bet

SUBMITTER: Shevket SH 

PROVIDER: S-EPMC6204919 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature