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PDBsum entry 4jnu

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protein Protein-protein interface(s) links
Transport protein PDB id
4jnu

 

 

 

 

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Contents
Protein chains
40 a.a.
Waters ×132
PDB id:
4jnu
Name: Transport protein
Title: Crystal structure of the human nup57ccs3 Coiled-coil segment, space group p21
Structure: Nucleoporin p54. Chain: a, b, c, d. Fragment: unp residues 453-491. Synonym: nup54, 54 kda nucleoporin. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: nup54. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.45Å     R-factor:   0.186     R-free:   0.218
Authors: T.Stuwe,C.J.Bley,D.J.Mayo,A.Hoelz
Key ref: T.Stuwe et al. (2015). Architecture of the fungal nuclear pore inner ring complex. Science, 350, 56-64. PubMed id: 26316600 DOI: 10.1126/science.aac9176
Date:
15-Mar-13     Release date:   17-Sep-14    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q7Z3B4  (NUP54_HUMAN) -  Nucleoporin p54 from Homo sapiens
Seq:
Struc:
507 a.a.
40 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1126/science.aac9176 Science 350:56-64 (2015)
PubMed id: 26316600  
 
 
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.
 

 

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