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PDBsum entry 4rxh

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protein ligands links
Transport protein PDB id
4rxh
Jmol PyMol
Contents
Protein chain
421 a.a.
Ligands
LYS-LYS-ARG-LYS-
VAL
PRO-PRO-LYS-LYS-
LYS-ARG-LYS-VAL
Waters ×349
PDB id:
4rxh
Name: Transport protein
Title: Crystal structure of importin-alpha from neurospora crassa c with sv40nls
Structure: Importin subunit alpha. Chain: b. Engineered: yes. Large t antigen. Chain: a, c. Synonym: lt, lt-ag. Engineered: yes
Source: Neurospora crassa. Organism_taxid: 5141. Strain: fgsc 9718. Gene: 3h10.030. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Simian virus 40. Sv40.
Resolution:
1.76Å     R-factor:   0.184     R-free:   0.211
Authors: N.E.Bernardes,A.A.S.Takeda,M.R.M.Fontes
Key ref: N.E.Bernardes et al. (2015). Structure of Importin-α from a Filamentous Fungus in Complex with a Classical Nuclear Localization Signal. PLoS One, 10, e0128687. PubMed id: 26091498 DOI: 10.1371/journal.pone.0128687
Date:
11-Dec-14     Release date:   01-Jul-15    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9C2K9  (Q9C2K9_NEUCS) -  Importin subunit alpha
Seq:
Struc:
 
Seq:
Struc:
548 a.a.
421 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: E.C.3.6.4.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   2 terms 
  Biological process     protein import into nucleus   1 term 
  Biochemical function     protein transporter activity     1 term  

 

 
DOI no: 10.1371/journal.pone.0128687 PLoS One 10:e0128687 (2015)
PubMed id: 26091498  
 
 
Structure of Importin-α from a Filamentous Fungus in Complex with a Classical Nuclear Localization Signal.
N.E.Bernardes, A.A.Takeda, T.R.Dreyer, F.Z.Freitas, M.C.Bertolini, M.R.Fontes.
 
  ABSTRACT  
 
Neurospora crassa is a filamentous fungus that has been extensively studied as a model organism for eukaryotic biology, providing fundamental insights into cellular processes such as cell signaling, growth and differentiation. To advance in the study of this multicellular organism, an understanding of the specific mechanisms for protein transport into the cell nucleus is essential. Importin-α (Imp-α) is the receptor for cargo proteins that contain specific nuclear localization signals (NLSs) that play a key role in the classical nuclear import pathway. Structures of Imp-α from different organisms (yeast, rice, mouse, and human) have been determined, revealing that this receptor possesses a conserved structural scaffold. However, recent studies have demonstrated that the Impα mechanism of action may vary significantly for different organisms or for different isoforms from the same organism. Therefore, structural, functional, and biophysical characterization of different Impα proteins is necessary to understand the selectivity of nuclear transport. Here, we determined the first crystal structure of an Impα from a filamentous fungus which is also the highest resolution Impα structure already solved to date (1.75 Å). In addition, we performed calorimetric analysis to determine the affinity and thermodynamic parameters of the interaction between Imp-α and the classical SV40 NLS peptide. The comparison of these data with previous studies on Impα proteins led us to demonstrate that N. crassa Imp-α possess specific features that are distinct from mammalian Imp-α but exhibit important similarities to rice Imp-α, particularly at the minor NLS binding site.
 

 

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