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PDBsum entry 3eab
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Contents |
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(+ 0 more)
89 a.a.
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40 a.a.
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39 a.a.
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41 a.a.
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37 a.a.
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38 a.a.
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37 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 basis for midbody targeting of spastin by the escrt-Iii protein chmp1b.
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Authors
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D.Yang,
N.Rismanchi,
B.Renvoisé,
J.Lippincott-Schwartz,
C.Blackstone,
J.H.Hurley.
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Ref.
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Nat Struct Biol, 2008,
15,
1278-1286.
[DOI no: ]
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PubMed id
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Abstract
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The endosomal sorting complex required for transport (ESCRT) machinery,
including ESCRT-III, localizes to the midbody and participates in the
membrane-abscission step of cytokinesis. The ESCRT-III protein charged
multivesicular body protein 1B (CHMP1B) is required for recruitment of the MIT
domain-containing protein spastin, a microtubule-severing enzyme, to the
midbody. The 2.5-A structure of the C-terminal tail of CHMP1B with the MIT
domain of spastin reveals a specific, high-affinity complex involving a
noncanonical binding site between the first and third helices of the MIT domain.
The structural interface is twice as large as that of the MIT domain of the
VPS4-CHMP complex, consistent with the high affinity of the interaction. A
series of unique hydrogen-bonding interactions and close packing of small side
chains discriminate against the other ten human ESCRT-III subunits. Point
mutants in the CHMP1B binding site of spastin block recruitment of spastin to
the midbody and impair cytokinesis.
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Figure 3.
(a) Overall structure of the MIT domain (blue) and CHMP1B
(orange). (b) Key MIM leucine residues bind to hydrophobic
pockets in the groove between  1
and 3
of the MIT domain. The spastin MIT domain surface is colored
green for carbon atoms, red for oxygen and blue for nitrogen.
Contiguous green regions indicate hydrophobic surfaces. (c)
Overview of polar interactions between CHMP1B-CTR and the
spastin MIT domain. (d–f) Details of interactions as seen in
insets d–f within c.
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Figure 5.
(a) HeLa cells expressing wild-type (WT) Myc-spastin (above,
green) or Myc–spastin-H120D F124D (below, green) were
co-immunostained for Myc epitope and  -tubulin.
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
Nat Struct Biol
(2008,
15,
1278-1286)
copyright 2008.
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