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• W4360866976 abstract "Abstract G-proteins function as molecular switches to power cofactor translocation and confer fidelity in metal trafficking. MMAA, a G-protein motor, together with MMAB, an adenosyltransferase, orchestrate cofactor delivery and repair of B 12 -dependent human methylmalonyl-CoA mutase (MMUT). The mechanism by which the motor assembles and moves a >1300 Da cargo, or fails in disease, are poorly understood. Herein, we report the crystal structure of the human MMUT-MMAA nanomotor assembly, which reveals a dramatic 180° rotation of the B 12 domain, exposing it to solvent. The nanomotor complex, stabilized by MMAA wedging between two MMUT domains, leads to ordering of the switch I and III loops, revealing the molecular basis of mutase-dependent GTPase activation. The structure explains the biochemical penalties incurred by methylmalonic aciduria-causing mutations that reside at the newly identified MMAA-MMUT interfaces." @default.
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• W4360866976 date "2023-03-23" @default.
• W4360866976 modified "2023-09-29" @default.
• W4360866976 title "Architecture of the human G-protein-methylmalonyl-CoA mutase nanoassembly for B₁₂delivery and repair" @default.
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• W4360866976 doi "https://doi.org/10.1101/2023.03.23.533963" @default.
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