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The structure of Tim50(164-361) suggests the mechanism by which Tim50 receives
mitochondrial presequences
#MMPMID26323300
Li J
; Sha B
Acta Crystallogr F Struct Biol Commun
2015[Sep]; 71
(Pt 9
): 1146-51
PMID26323300
show ga
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
?-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 presequence
helix by utilizing the inner side of the protruding ?-hairpin through hydrophobic
interactions. Therefore, the protruding ?-hairpin of Tim50 may play critical
roles in receiving the presequence and recruiting Tim23 for subsequent protein
translocations.
|Amino Acid Sequence
[MESH]
|Crystallization
[MESH]
|Crystallography, X-Ray
[MESH]
|Mitochondria/*metabolism
[MESH]
|Mitochondrial Membrane Transport Proteins/*chemistry/*metabolism
[MESH]
|Mitochondrial Precursor Protein Import Complex Proteins
[MESH]
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