8Q4H
a membrane-bound menaquinol:organohalide oxidoreductase complex RDH complex
Summary for 8Q4H
| Entry DOI | 10.2210/pdb8q4h/pdb |
| EMDB information | 18148 |
| Descriptor | Tetrachloroethene reductive dehalogenase, Probable tetrachloroethene reductive dehalogenase membrane anchor protein, (~{Z})-1,2-bis(chloranyl)ethene, ... (7 entities in total) |
| Functional Keywords | rdh menaquinol:organohalide oxidoreductase, electron transport |
| Biological source | Desulfitobacterium hafniense TCE1 More |
| Total number of polymer chains | 4 |
| Total formula weight | 139082.84 |
| Authors | Dongchun, N.,Ekundayo, B.,Henning, S.,Julien, M.,Holliger, C.,Cimmino, L. (deposition date: 2023-08-07, release date: 2023-10-18, Last modification date: 2023-11-15) |
| Primary citation | Cimmino, L.,Duarte, A.G.,Ni, D.,Ekundayo, B.E.,Pereira, I.A.C.,Stahlberg, H.,Holliger, C.,Maillard, J. Structure of a membrane-bound menaquinol:organohalide oxidoreductase. Nat Commun, 14:7038-7038, 2023 Cited by PubMed Abstract: Organohalide-respiring bacteria are key organisms for the bioremediation of soils and aquifers contaminated with halogenated organic compounds. The major players in this process are respiratory reductive dehalogenases, corrinoid enzymes that use organohalides as substrates and contribute to energy conservation. Here, we present the structure of a menaquinol:organohalide oxidoreductase obtained by cryo-EM. The membrane-bound protein was isolated from Desulfitobacterium hafniense strain TCE1 as a PceAB complex catalysing the dechlorination of tetrachloroethene. Two catalytic PceA subunits are anchored to the membrane by two small integral membrane PceB subunits. The structure reveals two menaquinone molecules bound at the interface of the two different subunits, which are the starting point of a chain of redox cofactors for electron transfer to the active site. In this work, the structure elucidates how energy is conserved during organohalide respiration in menaquinone-dependent organohalide-respiring bacteria. PubMed: 37923808DOI: 10.1038/s41467-023-42927-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.83 Å) |
Structure validation
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