Architecture of the Heme-translocating CcmABCD/E complex required for Cytochrome c maturation

Lorena Ilcu, Lukas Denkhaus, Anton Brausemann, Lin Zhang () and Oliver Einsle ()
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Lorena Ilcu: Institut für Biochemie
Lukas Denkhaus: Institut für Biochemie
Anton Brausemann: Institut für Biochemie
Lin Zhang: Institut für Biochemie
Oliver Einsle: Institut für Biochemie

Nature Communications, 2023, vol. 14, issue 1, 1-10

Abstract: Abstract Mono- and multiheme cytochromes c are post-translationally matured by the covalent attachment of heme. For this, Escherichia coli employs the most complex type of maturation machineries, the Ccm-system (for cytochrome c maturation). It consists of two membrane protein complexes, one of which shuttles heme across the membrane to a mobile chaperone that then delivers the cofactor to the second complex, an apoprotein:heme lyase, for covalent attachment. Here we report cryo-electron microscopic structures of the heme translocation complex CcmABCD from E. coli, alone and bound to the heme chaperone CcmE. CcmABCD forms a heterooctameric complex centered around the ABC transporter CcmAB that does not by itself transport heme. Our data suggest that the complex flops a heme group from the inner to the outer leaflet at its CcmBC interfaces, driven by ATP hydrolysis at CcmA. A conserved heme-handling motif (WxWD) at the periplasmic side of CcmC rotates the heme by 90° for covalent attachment to the heme chaperone CcmE that we find interacting exclusively with the CcmB subunit.

Date: 2023
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DOI: 10.1038/s41467-023-40881-y

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