7F02
Cytochrome c-type biogenesis protein CcmABCD from E. coli
Summary for 7F02
| Entry DOI | 10.2210/pdb7f02/pdb |
| EMDB information | 31394 |
| Descriptor | Cytochrome c biogenesis ATP-binding export protein CcmA, Heme exporter protein B, Heme exporter protein C, ... (7 entities in total) |
| Functional Keywords | atp-binding exporter, heme transmembrane transporter, cytochrome c biogenesis protein., membrane protein |
| Biological source | Escherichia coli BL21(DE3) More |
| Total number of polymer chains | 6 |
| Total formula weight | 130076.76 |
| Authors | |
| Primary citation | Li, J.,Zheng, W.,Gu, M.,Han, L.,Luo, Y.,Yu, K.,Sun, M.,Zong, Y.,Ma, X.,Liu, B.,Lowder, E.P.,Mendez, D.L.,Kranz, R.G.,Zhang, K.,Zhu, J. Structures of the CcmABCD heme release complex at multiple states. Nat Commun, 13:6422-6422, 2022 Cited by PubMed Abstract: Cytochromes c use heme as a cofactor to carry electrons in respiration and photosynthesis. The cytochrome c maturation system I, consisting of eight membrane proteins (CcmABCDEFGH), results in the attachment of heme to cysteine residues of cytochrome c proteins. Since all c-type cytochromes are periplasmic, heme is first transported to a periplasmic heme chaperone, CcmE. A large membrane complex, CcmABCD has been proposed to carry out this transport and linkage to CcmE, yet the structural basis and mechanisms underlying the process are unknown. We describe high resolution cryo-EM structures of CcmABCD in an unbound form, in complex with inhibitor AMP-PNP, and in complex with ATP and heme. We locate the ATP-binding site in CcmA and the heme-binding site in CcmC. Based on our structures combined with functional studies, we propose a hypothetic model of heme trafficking, heme transfer to CcmE, and ATP-dependent release of holoCcmE from CcmABCD. CcmABCD represents an ABC transporter complex using the energy of ATP hydrolysis for the transfer of heme from one binding partner (CcmC) to another (CcmE). PubMed: 36307425DOI: 10.1038/s41467-022-34136-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.24 Å) |
Structure validation
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