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![[Figure 3]](ih5004fig3mag.jpg)
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Figure 3
The role of NDUFAF1 in the assembly process of complex I from Y. lipolytica. (a, b) In the late PP module intermediate, the TMH1–2 loop of the ND3 subunit with its conserved cysteine is bound in a binding cleft of NDUFAF1. (c, d) In mature complex I, the same loop is bound at the interface between the membrane and peripheral arms, mainly formed by the central subunits NDUFS2, NDUFS7 and ND1. In this conformation the cysteine is close to the Q-binding cavity (∼6 Å) and the conserved Tyr144NDUFS2 (∼17 Å), a residue critical for binding ubiquinone near Fe–S cluster N2 (Tocilescu et al., 2010  ). The conformational change of the TMH1–2 loop of ND3 upon complex I maturation is accompanied by major shifts of TMH1ND3 and TMH4ND6 (yellow and orange arrows, respectively). (e) View from the matrix side of the PP module. TMH1ND3 and TMH4ND6 change their positions upon maturation as their binding sites in the assembly intermediate (left) overlap with the binding sites of TMH16ND5 and TMH1NDUFA11 of the PD module (right). Assembly factors and accessory subunits, except NDUFA11, are omitted for clarity. (e) is adapted from Schiller et al. (2022). |
![[Figure 3]](ih5004fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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