Structural highlights
Publication Abstract from PubMed
The covalent attachment of one or multiple heme cofactors to cytochrome c protein chains enables cytochrome c proteins to be used in electron transfer and redox catalysis in extracytoplasmic environments. A dedicated heme maturation machinery, whose core component is a heme lyase, scans nascent peptides after Sec-dependent translocation for CXnCH-binding motifs. Here we report the three-dimensional (3D) structure of the heme lyase CcmF, a 643-amino acid integral membrane protein, from Thermus thermophilus. CcmF contains a heme b cofactor at the bottom of a large cavity that opens toward the extracellular side to receive heme groups from the heme chaperone CcmE for cytochrome maturation. A surface groove on CcmF may guide the extended apoprotein to heme attachment at or near a loop containing the functionally essential WXWD motif, which is situated above the putative cofactor binding pocket. The structure suggests heme delivery from within the membrane, redefining the role of the chaperone CcmE.
Architecture of the membrane-bound cytochrome c heme lyase CcmF.,Brausemann A, Zhang L, Ilcu L, Einsle O Nat Chem Biol. 2021 May 6. pii: 10.1038/s41589-021-00793-8. doi:, 10.1038/s41589-021-00793-8. PMID:33958791[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Brausemann A, Zhang L, Ilcu L, Einsle O. Architecture of the membrane-bound cytochrome c heme lyase CcmF. Nat Chem Biol. 2021 May 6. pii: 10.1038/s41589-021-00793-8. doi:, 10.1038/s41589-021-00793-8. PMID:33958791 doi:http://dx.doi.org/10.1038/s41589-021-00793-8
