6q9d | pdb_00006q9d

CI Peripheral Arm focused refinement from Ovine respiratory SC I+III2

spinqualitylabelsall models 6q9d, resolution 3.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6q9d is a 18 chain structure with sequence from Ovis aries. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FES, FMN, NDP, SF4, ZMP, ZN Related: 6q9b Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [W5NQT7_SHEEP] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[RuleBase:RU000722] [B9VGZ9_SHEEP] 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] [W5QAH8_SHEEP] 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:PIRNR005822] Publication Abstract from PubMed The mitochondrial electron transport chain complexes are organized into supercomplexes (SCs) of defined stoichiometry, which have been proposed to regulate electron flux via substrate channeling. We demonstrate that CoQ trapping in the isolated SC I+III2 limits complex (C)I turnover, arguing against channeling. The SC structure, resolved at up to 3.8 A in four distinct states, suggests that CoQ oxidation may be rate limiting because of unequal access of CoQ to the active sites of CIII2. CI shows a transition between "closed" and "open" conformations, accompanied by the striking rotation of a key transmembrane helix. Furthermore, the state of CI affects the conformational flexibility within CIII2, demonstrating crosstalk between the enzymes. CoQ was identified at only three of the four binding sites in CIII2, suggesting that interaction with CI disrupts CIII2 symmetry in a functionally relevant manner. Together, these observations indicate a more nuanced functional role for the SCs. Structures of Respiratory Supercomplex I+III2 Reveal Functional and Conformational Crosstalk.,Letts JA, Fiedorczuk K, Degliesposti G, Skehel M, Sazanov LA Mol Cell. 2019 Sep 19;75(6):1131-1146.e6. doi: 10.1016/j.molcel.2019.07.022. Epub, 2019 Sep 3. PMID:31492636 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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