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Structure paper

TitleStructures of the CcmABCD heme release complex at multiple states.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 6422, Year 2022
Publish dateOct 28, 2022
AuthorsJiao 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 / Jiapeng Zhu /
PubMed AbstractCytochromes 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 ...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).
External linksNat Commun / PubMed:36307425 / PubMed Central
MethodsEM (single particle)
Resolution2.86 - 4.03 Å
Structure data

31394

7f02

EMDB-31394, PDB-7f02:
Cytochrome c-type biogenesis protein CcmABCD from E. coli
Method: EM (single particle) / Resolution: 3.24 Å

31395

7f03

EMDB-31395, PDB-7f03:
Cytochrome c-type biogenesis protein CcmABCD from E. coli in complex with ANP
Method: EM (single particle) / Resolution: 3.29 Å

31396

7f04

EMDB-31396, PDB-7f04:
Cytochrome c-type biogenesis protein CcmABCD from E. coli in complex with Heme and ATP.
Method: EM (single particle) / Resolution: 2.86 Å

31956

7vfj

EMDB-31956, PDB-7vfj:
Cytochrome c-type biogenesis protein CcmABCD
Method: EM (single particle) / Resolution: 3.98 Å

31957

7vfp

EMDB-31957, PDB-7vfp:
Cytochrome c-type biogenesis protein CcmABCD from E. coli in complex with heme and single ATP
Method: EM (single particle) / Resolution: 4.03 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

ChemComp-3PE:
1,2-Distearoyl-sn-glycerophosphoethanolamine / phospholipid*YM

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-HOH:
WATER

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

Source
  • escherichia coli bl21(de3) (bacteria)
KeywordsMEMBRANE PROTEIN / ATP-binding exporter / Heme transmembrane transporter / Cytochrome c biogenesis protein. / Cytochrome c biogenesis protein

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