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PDBsum entry 1v92
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Recombination
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PDB id
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1v92
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure, Dynamics and interactions of p47, A major adaptor of the aaa atpase, P97.
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Authors
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X.Yuan,
P.Simpson,
C.Mckeown,
H.Kondo,
K.Uchiyama,
R.Wallis,
I.Dreveny,
C.Keetch,
X.Zhang,
C.Robinson,
P.Freemont,
S.Matthews.
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Ref.
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EMBO J, 2004,
23,
1463-1473.
[DOI no: ]
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PubMed id
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Abstract
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p47 is a major adaptor molecule of the cytosolic AAA ATPase p97. The principal
role of the p97-p47 complex is in regulation of membrane fusion events.
Mono-ubiquitin recognition by p47 has also been shown to be crucial in the
p97-p47-mediated Golgi membrane fusion events. Here, we describe the
high-resolution solution structures of the N-terminal UBA domain and the central
domain (SEP) from p47. The p47 UBA domain has the characteristic three-helix
bundle fold and forms a highly stable complex with ubiquitin. We report the
interaction surfaces of the two proteins and present a structure for the p47
UBA-ubiquitin complex. The p47 SEP domain adopts a novel fold with a
betabetabetaalphaalphabeta secondary structure arrangement, where beta4 pairs in
a parallel fashion to beta1. Based on biophysical studies, we demonstrate a
clear propensity for the self-association of p47. Furthermore, p97 N binding
abolishes p47 self-association, revealing the potential interaction surfaces for
recognition of other domains within p97 or the substrate.
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Figure 1.
Figure 1 Schematic representation of the domain structure of
full-length rat p47 and fragments used in this study.
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Figure 4.
Figure 4 Comparison of p47 UBA -ubiquitin, CUE -ubiquitin and
di-ubiquitin structures. (A) C[  ]traces
representing the superimposition of the 10 refined p47 UBA
-ubiquitin complex structures using the HADDOCK approach. p47
UBA is shown in gold and ubiquitin in green. (B) Ribbon
representation of the p47 UBA -ubiquitin complex. (C) Ribbon
representation of the structure of the yeast CUE2-1 domain
-ubiquitin complex in the same orientation as in (B). The CUE
domain is shown in purple (Kang et al, 2003; Shih et al, 2003).
(D) Ribbon representation of the structure of Lys48-linked
di-ubiquitin in the same orientation as in (B) (Cook et al,
1992, 1994; Cummings et al, 1995; Beal et al, 1998; Phillips et
al, 2001; Varadan et al, 2002).
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2004,
23,
1463-1473)
copyright 2004.
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