The structure of Tim50(164-361) suggests the mechanism by which Tim50 receives mitochondrial presequences

Acta Crystallographica. Section F, Structural Biology Communications
Jingzhi Li, Bingdong Sha

Abstract

Mitochondrial preproteins are transported through the translocase of the outer membrane (TOM) complex. Tim50 and Tim23 then transfer preproteins with N-terminal targeting presequences through the intermembrane space (IMS) across the inner membrane. The crystal structure of the IMS domain of Tim50 [Tim50(164-361)] has previously been determined to 1.83 Å resolution. Here, the crystal structure of Tim50(164-361) at 2.67 Å resolution that was crystallized using a different condition is reported. Compared with the previously determined Tim50(164-361) structure, significant conformational changes occur within the protruding β-hairpin of Tim50 and the nearby helix A2. These findings indicate that the IMS domain of Tim50 exhibits significant structural plasticity within the putative presequence-binding groove, which may play important roles in the function of Tim50 as a receptor protein in the TIM complex that interacts with the presequence and multiple other proteins. More interestingly, the crystal packing indicates that helix A1 from the neighboring monomer docks into the putative presequence-binding groove of Tim50(164-361), which may mimic the scenario of Tim50 and the presequence complex. Tim50 may recognize and bind the presequ...Continue Reading

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Citations

Oct 24, 2018·Molecular and Cellular Biology·Himangshu S BoseRandy M Whittal
Mar 28, 2019·Gut Microbes·Dakota N Jackson, Arianne L Theiss
Feb 20, 2020·Biological Chemistry·Sylvie CallegariPeter Rehling
Jun 12, 2016·Biological Chemistry·Sebastian P StraubNikolaus Pfanner
Mar 19, 2020·Molecular Biology of the Cell·Srujan Kumar MattaPatrick D'Silva
Aug 8, 2021·International Journal of Molecular Sciences·Minu ChaudhuriFidel Soto Gonzalez

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