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PDBsum entry 4xzv
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Contents |
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416 a.a.
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142 a.a.
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133 a.a.
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References listed in PDB file
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Key reference
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Title
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Structural insight into the triap1/preli-Like domain family of mitochondrial phospholipid transfer complexes.
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Authors
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X.Miliara,
J.A.Garnett,
T.Tatsuta,
F.Abid ali,
H.Baldie,
I.Pérez-Dorado,
P.Simpson,
E.Yague,
T.Langer,
S.Matthews.
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Ref.
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Embo Rep, 2015,
16,
824-835.
[DOI no: ]
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PubMed id
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Abstract
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The composition of the mitochondrial membrane is important for its architecture
and proper function. Mitochondria depend on a tightly regulated supply of
phospholipid via intra-mitochondrial synthesis and by direct import from the
endoplasmic reticulum. The Ups1/PRELI-like family together with its
mitochondrial chaperones (TRIAP1/Mdm35) represent a unique heterodimeric lipid
transfer system that is evolutionary conserved from yeast to man. Work presented
here provides new atomic resolution insight into the function of a human member
of this system. Crystal structures of free TRIAP1 and the TRIAP1-SLMO1 complex
reveal how the PRELI domain is chaperoned during import into the intermembrane
mitochondrial space. The structural resemblance of PRELI-like domain of SLMO1
with that of mammalian phoshatidylinositol transfer proteins (PITPs) suggest
that they share similar lipid transfer mechanisms, in which access to a buried
phospholipid-binding cavity is regulated by conformationally adaptable loops.
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