 |
PDBsum entry 5cws
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Protein transport
|
PDB id
|
|
|
|
5cws
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
208 a.a.
|
 |
|
|
|
|
|
|
|
223 a.a.
|
 |
|
|
|
|
|
|
|
169 a.a.
|
 |
|
|
|
|
|
|
|
180 a.a.
|
 |
|
|
|
|
|
|
|
241 a.a.
|
 |
|
|
|
|
|
|
|
40 a.a.
|
 |
|
|
|
|
|
|
|
|
|
PDB id:
|
 |
|
 |
| Name: |
 |
Protein transport
|
 |
|
Title:
|
 |
Crystal structure of the intact chaetomium thermophilum nsp1-nup49- nup57 channel nucleoporin heterotrimer bound to its nic96 nuclear pore complex attachment site
|
|
Structure:
|
 |
Sab-158 fab light chain. Chain: a, g. Engineered: yes. Sab-158 fab heavy chain. Chain: b, h. Engineered: yes. Nucleoporin nsp1. Chain: c, i. Fragment: unp residues 467-674.
|
|
Source:
|
 |
Homo sapiens. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Chaetomium thermophilum (strain dsm 1495 / cbs 144.50 / imi 039719). Organism_taxid: 759272. Strain: dsm 1495 / cbs 144.50 / imi 039719. Gene: nsp1, ctht_0054390.
|
|
Resolution:
|
 |
|
3.77Å
|
R-factor:
|
0.231
|
R-free:
|
0.265
|
|
|
Authors:
|
 |
C.J.Bley,S.Petrovic,M.Paduch,V.Lu,A.A.Kossiakoff,A.Hoelz
|
|
Key ref:
|
 |
T.Stuwe
et al.
(2015).
Architecture of the fungal nuclear pore inner ring complex.
Science,
350,
56-64.
PubMed id:
DOI:
|
 |
|
Date:
|
 |
|
28-Jul-15
|
Release date:
|
14-Oct-15
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
Headers
|
 |
|
|
References
|
|
|
|
|
|
|
No UniProt id for this chain
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
No UniProt id for this chain
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
G0SBQ3
(NSP1_CHATD) -
Nucleoporin NSP1 from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
678 a.a.
169 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
G0S4X2
(NUP49_CHATD) -
Nucleoporin NUP49 from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
470 a.a.
180 a.a.*
|
|
|
|
|
|
|
|
|
 |
 |
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
| |
|
DOI no:
|
Science
350:56-64
(2015)
|
|
PubMed id:
|
|
|
|
|
| |
|
Architecture of the fungal nuclear pore inner ring complex.
|
|
T.Stuwe,
C.J.Bley,
K.Thierbach,
S.Petrovic,
S.Schilbach,
D.J.Mayo,
T.Perriches,
E.J.Rundlet,
Y.E.Jeon,
L.N.Collins,
F.M.Huber,
D.H.Lin,
M.Paduch,
A.Koide,
V.Lu,
J.Fischer,
E.Hurt,
S.Koide,
A.A.Kossiakoff,
A.Hoelz.
|
|
|
|
| |
ABSTRACT
|
|
|
| |
|
The nuclear pore complex (NPC) constitutes the sole gateway for bidirectional
nucleocytoplasmic transport. We present the reconstitution and interdisciplinary
analyses of the ~425-kilodalton inner ring complex (IRC), which forms the
central transport channel and diffusion barrier of the NPC, revealing its
interaction network and equimolar stoichiometry. The Nsp1•Nup49•Nup57
channel nucleoporin heterotrimer (CNT) attaches to the IRC solely through the
adaptor nucleoporin Nic96. The CNT•Nic96 structure reveals that Nic96
functions as an assembly sensor that recognizes the three-dimensional
architecture of the CNT, thereby mediating the incorporation of a defined CNT
state into the NPC. We propose that the IRC adopts a relatively rigid scaffold
that recruits the CNT to primarily form the diffusion barrier of the NPC, rather
than enabling channel dilation.
|
|
|
|
|
|
|
 |
 |
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
');
}
}
| | |