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PDBsum entry 6gci
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Membrane protein
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PDB id
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6gci
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References listed in PDB file
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Key reference
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Title
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The molecular mechanism of transport by the mitochondrial ADP/ATP carrier.
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Authors
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J.J.Ruprecht,
M.S.King,
T.Zögg,
A.A.Aleksandrova,
E.Pardon,
P.G.Crichton,
J.Steyaert,
E.R.S.Kunji.
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Ref.
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Cell, 2019,
176,
435.
[DOI no: ]
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PubMed id
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Abstract
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Mitochondrial ADP/ATP carriers transport ADP into the mitochondrial matrix for
ATP synthesis, and ATP out to fuel the cell, by cycling between cytoplasmic-open
and matrix-open states. The structure of the cytoplasmic-open state is known,
but it has proved difficult to understand the transport mechanism in the absence
of a structure in the matrix-open state. Here, we describe the structure of the
matrix-open state locked by bongkrekic acid bound in the ADP/ATP-binding site at
the bottom of the central cavity. The cytoplasmic side of the carrier is closed
by conserved hydrophobic residues, and a salt bridge network, braced by
tyrosines. Glycine and small amino acid residues allow close-packing of helices
on the matrix side. Uniquely, the carrier switches between states by rotation of
its three domains about a fulcrum provided by the substrate-binding site.
Because these features are highly conserved, this mechanism is likely to apply
to the whole mitochondrial carrier family. VIDEO ABSTRACT.
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