ArticleJournal of molecular biology2018
Structurally Mapping Endogenous Heme in the CcmCDE Membrane Complex for Cytochrome c Biogenesis.
Article in Journal of molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Analysis of putative heme ligands in the System I bacterial cytochromeMicrobiology spectrum · 2026Article
- From genes to function: regulation, maturation, and evolution of cytochromeApplied and environmental microbiology · 2025Review
- Article
- Structural Insights into Mechanisms Underlying Mitochondrial and Bacterial Cytochrome c Synthases.Biomolecules · 2024Article
- Article
- Helicobacter pylori and Campylobacter jejuni bacterial holocytochrome c synthase structure-function analysis reveals conservation of heme binding.Communications biology · 2024Article
- Assembly of Protein Complexes in and on the Membrane with Predicted Spatial Arrangement Constraints.Journal of molecular biology · 2024Article
- Recombinant Biogenesis and Analysis of Cytochrome c Species.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Assembly of Protein Complexes In and On the Membrane with Predicted Spatial Arrangement Constraints.bioRxiv : the preprint server for biology · 2023Article
- Structural basis of membrane machines that traffick and attach heme to cytochromes.The Journal of biological chemistry · 2023Article
- Structures of the CcmABCD heme release complex at multiple states.Nature communications · 2022Article
- AF2Complex predicts direct physical interactions in multimeric proteins with deep learning.Nature communications · 2022Article
- Cryo-EM of CcsBA reveals the basis for cytochrome c biogenesis and heme transport.Nature chemical biology · 2022Article
- In vitro reconstitution reveals major differences between human and bacterial cytochrome c synthases.eLife · 2021Article
- The OXA2a Insertase of Arabidopsis Is Required for CytochromePlant physiology · 2020Article
- Article
- The CcmC-CcmE interaction during cytochromeThe Journal of biological chemistry · 2018Article
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5 authors.
Funding
Abstract
Although many putative heme transporters have been discovered, it has been challenging to prove that these proteins are directly involved with heme trafficking in vivo and to identify their heme binding domains. The prokaryotic pathways for cytochrome c biogenesis, Systems I and II, transport heme from inside the cell to outside for stereochemical attachment to cytochrome c, making them excellent models to study heme trafficking. System I is composed of eight integral membrane proteins (CcmA-H) and is proposed to transport heme via CcmC to an external "WWD" domain for presentation to the membrane-tethered heme chaperone, CcmE. Herein, we develop a new cysteine/heme crosslinking approach to trap and map endogenous heme in CcmC (WWD domain) and CcmE (defining "2-vinyl" and "4-vinyl" pockets for heme). Crosslinking occurs when either of the two vinyl groups of heme localize near a thiol of an engineered cysteine residue. Double crosslinking, whereby both vinyls crosslink to two engineered cysteines, facilitated a more detailed structural mapping of the heme binding sites, including stereospecificity. Using heme crosslinking results, heme ligand identification, and genomic coevolution data, we model the structure of the CcmCDE complex, including the WWD heme binding domain. We conclude that CcmC trafficks heme via its WWD domain and propose the structural basis for stereochemical attachment of heme.
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