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PDBsum entry 4xiz
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Lipid transport/oxidoreductase
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PDB id
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4xiz
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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 basis of intramitochondrial phosphatidic acid transport mediated by ups1-Mdm35 complex.
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Authors
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F.Yu,
F.He,
H.Yao,
C.Wang,
J.Wang,
J.Li,
X.Qi,
H.Xue,
J.Ding,
P.Zhang.
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Ref.
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Embo Rep, 2015,
16,
813-823.
[DOI no: ]
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PubMed id
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Abstract
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Ups1 forms a complex with Mdm35 and is critical for the transport of
phosphatidic acid (PA) from the mitochondrial outer membrane to the inner
membrane. We report the crystal structure of the Ups1-Mdm35-PA complex and the
functional characterization of Ups1-Mdm35 in PA binding and transfer. Ups1
features a barrel-like structure consisting of an antiparallel β-sheet and
three α-helices. Mdm35 adopts a three-helical clamp-like structure to wrap
around Ups1 to form a stable complex. The β-sheet and α-helices of Ups1 form a
long tunnel-like pocket to accommodate the substrate PA, and a short helix α2
acts as a lid to cover the pocket. The hydrophobic residues lining the pocket
and helix α2 are critical for PA binding and transfer. In addition, a
hydrophilic patch on the surface of Ups1 near the PA phosphate-binding site also
plays an important role in the function of Ups1-Mdm35. Our study reveals the
molecular basis of the function of Ups1-Mdm35 and sheds new light on the
mechanism of intramitochondrial phospholipid transport by the MSF1/PRELI family
proteins.
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