Structural highlights
Function
[Q9UUU2_YARLL] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain.[RuleBase:RU364066] [A0A1D8NG21_YARLL] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[RuleBase:RU000722] [NU6M_YARLI] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. [A0A1H6PXT9_YARLL] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[RuleBase:RU000722] [A0A1D8N5V2_YARLL] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[RuleBase:RU363103] [S5TF58_YARLL] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[RuleBase:RU003404] [NU4LM_YARLI] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. [S5TMP9_YARLL] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[RuleBase:RU003297] [S5TMS4_YARLL] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[RuleBase:RU003640][SAAS:SAAS01013641] [A0A371C2D0_YARLL] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[PIRNR:PIRNR017016]
Publication Abstract from PubMed
Respiratory complex I is a redox-driven proton pump, accounting for a large part of the electrochemical gradient that powers mitochondrial adenosine triphosphate synthesis. Complex I dysfunction is associated with severe human diseases. Assembly of the one-megadalton complex I in the inner mitochondrial membrane requires assembly factors and chaperones. We have determined the structure of complex I from the aerobic yeast Yarrowia lipolytica by electron cryo-microscopy at 3.2-A resolution. A ubiquinone molecule was identified in the access path to the active site. The electron cryo-microscopy structure indicated an unusual lipid-protein arrangement at the junction of membrane and matrix arms that was confirmed by molecular simulations. The structure of a complex I mutant and an assembly intermediate provide detailed molecular insights into the cause of a hereditary complex I-linked disease and complex I assembly in the inner mitochondrial membrane.
High-resolution cryo-EM structures of respiratory complex I: Mechanism, assembly, and disease.,Parey K, Haapanen O, Sharma V, Kofeler H, Zullig T, Prinz S, Siegmund K, Wittig I, Mills DJ, Vonck J, Kuhlbrandt W, Zickermann V Sci Adv. 2019 Dec 11;5(12):eaax9484. doi: 10.1126/sciadv.aax9484. eCollection, 2019 Dec. PMID:31844670[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Parey K, Haapanen O, Sharma V, Kofeler H, Zullig T, Prinz S, Siegmund K, Wittig I, Mills DJ, Vonck J, Kuhlbrandt W, Zickermann V. High-resolution cryo-EM structures of respiratory complex I: Mechanism, assembly, and disease. Sci Adv. 2019 Dec 11;5(12):eaax9484. doi: 10.1126/sciadv.aax9484. eCollection, 2019 Dec. PMID:31844670 doi:http://dx.doi.org/10.1126/sciadv.aax9484
