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-Structure paper
タイトル | Architecture of the Heme-translocating CcmABCD/E complex required for Cytochrome c maturation. |
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ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 5190, Year 2023 |
掲載日 | 2023年8月25日 |
著者 | Lorena Ilcu / Lukas Denkhaus / Anton Brausemann / Lin Zhang / Oliver Einsle / |
PubMed 要旨 | Mono- and multiheme cytochromes c are post-translationally matured by the covalent attachment of heme. For this, Escherichia coli employs the most complex type of maturation machineries, the Ccm- ...Mono- and multiheme cytochromes c are post-translationally matured by the covalent attachment of heme. For this, Escherichia coli employs the most complex type of maturation machineries, the Ccm-system (for cytochrome c maturation). It consists of two membrane protein complexes, one of which shuttles heme across the membrane to a mobile chaperone that then delivers the cofactor to the second complex, an apoprotein:heme lyase, for covalent attachment. Here we report cryo-electron microscopic structures of the heme translocation complex CcmABCD from E. coli, alone and bound to the heme chaperone CcmE. CcmABCD forms a heterooctameric complex centered around the ABC transporter CcmAB that does not by itself transport heme. Our data suggest that the complex flops a heme group from the inner to the outer leaflet at its CcmBC interfaces, driven by ATP hydrolysis at CcmA. A conserved heme-handling motif (WxWD) at the periplasmic side of CcmC rotates the heme by 90° for covalent attachment to the heme chaperone CcmE that we find interacting exclusively with the CcmB subunit. |
リンク | Nat Commun / PubMed:37626034 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.47 - 3.94 Å |
構造データ | EMDB-16597, PDB-8ce1: EMDB-16599, PDB-8ce5: EMDB-16601, PDB-8ce8: EMDB-16602, PDB-8cea: |
化合物 | ChemComp-MG: ChemComp-ATP: |
由来 |
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キーワード | MEMBRANE PROTEIN / Cytochrome c maturation |