Structures of the CcmABCD heme release complex at multiple states

Jiao Li, Wan Zheng, Ming Gu, Long Han, Yanmei Luo, Koukou Yu, Mengxin Sun, Yuliang Zong, Xiuxiu Ma, Bing Liu, Ethan P. Lowder, Deanna L. Mendez, Robert G. Kranz (), Kai Zhang () and Jiapeng Zhu ()
Additional contact information
Jiao Li: Nanjing University of Chinese Medicine
Wan Zheng: Nanjing University of Chinese Medicine
Ming Gu: Nanjing University of Chinese Medicine
Long Han: Yale University
Yanmei Luo: Nanjing University of Chinese Medicine
Koukou Yu: Nanjing University of Chinese Medicine
Mengxin Sun: Nanjing University of Chinese Medicine
Yuliang Zong: Nanjing University of Chinese Medicine
Xiuxiu Ma: Nanjing University of Chinese Medicine
Bing Liu: Nanjing University of Chinese Medicine
Ethan P. Lowder: Washington University in St. Louis
Deanna L. Mendez: Washington University in St. Louis
Robert G. Kranz: Washington University in St. Louis
Kai Zhang: Yale University
Jiapeng Zhu: Nanjing University of Chinese Medicine

Nature Communications, 2022, vol. 13, issue 1, 1-13

Abstract: 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).

Date: 2022
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DOI: 10.1038/s41467-022-34136-5

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