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PDBsum entry 1z3h
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Protein transport
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PDB id
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1z3h
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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 structure of the nuclear export receptor cse1 in its cytosolic state reveals a closed conformation incompatible with cargo binding.
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Authors
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A.Cook,
E.Fernandez,
D.Lindner,
J.Ebert,
G.Schlenstedt,
E.Conti.
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Ref.
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Mol Cell, 2005,
18,
355-367.
[DOI no: ]
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PubMed id
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Abstract
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Cse1 mediates nuclear export of importin alpha, the nuclear localization signal
(NLS) import adaptor. We report the 3.1 A resolution structure of cargo-free
Cse1, representing this HEAT repeat protein in its cytosolic state. Cse1 is
compact, consisting of N- and C-terminal arches that interact to form a ring.
Comparison with the structure of cargo-bound Cse1 shows a major conformational
change leading to opening of the structure upon cargo binding. The largest
structural changes occur within a hinge region centered at HEAT repeat 8. This
repeat contains a conserved insertion that connects the RanGTP and importin
alpha contact sites and that is essential for binding. In the cargo-free state,
the RanGTP binding sites are occluded and the importin alpha sites are
distorted. Mutations that destabilize the N- to C-terminal interaction uncouple
importin alpha and Ran binding, suggesting that the closed conformation prevents
association with importin alpha.
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Figure 4.
Figure 4. The Ring-like Structure of Cse1 Opens up to
Assume a Horseshoe Shape upon Cargo Binding
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Figure 5.
Figure 5. The Intramolecular Interaction between the N- and
C-Terminal Arches Prevents Cargo Binding in the Absence of RanGTP
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2005,
18,
355-367)
copyright 2005.
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