 |
PDBsum entry 1wr0
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Protein transport
|
PDB id
|
|
|
|
1wr0
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structural characterization of the mit domain from human vps4b.
|
|
|
Authors
|
|
H.Takasu,
J.G.Jee,
A.Ohno,
N.Goda,
K.Fujiwara,
H.Tochio,
M.Shirakawa,
H.Hiroaki.
|
|
|
Ref.
|
|
Biochem Biophys Res Commun, 2005,
334,
460-465.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The microtubule interacting and trafficking (MIT) domain is a small protein
module of unknown function that is conserved in proteins of diverse function,
such as Vps4, sorting nexin 15 (SNX15), and spastin. One non-synonymous single
nucleotide polymorphism was reported, which results in a Ile58-to-Met (I58M)
substitution in hVps4b. Here, we have determined the solution structure of the
MIT domain isolated from the NH(2)-terminus of human Vps4b, an AAA-ATPase
involved in multivesicular body formation. The MIT domain adopts an
'up-and-down' three-helix bundle. Comparison with the sequences of other MIT
domains clearly shows that the residues involved in inter-helical contacts are
well conserved. The Ile58-to-Met substitution resulted a substantial thermal
instability. In addition, we found a shallow crevice between helices A and C
that may serve as a protein-binding site. We propose that the MIT domain serves
as a putative adaptor domain for the ESCRT-III complex involved in endosomal
trafficking.
|
|
|
|
|
|
|
