6ZMQ
Cytochrome c Heme Lyase CcmF
Summary for 6ZMQ
| Entry DOI | 10.2210/pdb6zmq/pdb |
| Descriptor | Cytochrome C-type biogenesis protein ccmF, PROTOPORPHYRIN IX CONTAINING FE, DODECYL-BETA-D-MALTOSIDE, ... (5 entities in total) |
| Functional Keywords | heme lyase cytochrome c maturation membrane protein cytochrome, membrane protein |
| Biological source | Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) |
| Total number of polymer chains | 1 |
| Total formula weight | 77273.72 |
| Authors | Brausemann, A.,Einsle, O. (deposition date: 2020-07-03, release date: 2021-05-19, Last modification date: 2024-05-15) |
| Primary citation | Brausemann, A.,Zhang, L.,Ilcu, L.,Einsle, O. Architecture of the membrane-bound cytochrome c heme lyase CcmF. Nat.Chem.Biol., 17:800-805, 2021 Cited by PubMed Abstract: 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 CXCH-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. PubMed: 33958791DOI: 10.1038/s41589-021-00793-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.67 Å) |
Structure validation
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