POP-OUT | CLOSE
Crystal structure of the spinach aquaporin SoPIP2;1 in an open conformation to 3.9 resolution
2B5F
Primary Citation

Structural mechanism of plant aquaporin gating.

Tornroth-Horsefield, S.,  Wang, Y.,  Hedfalk, K.,  Johanson, U.,  Karlsson, M.,  Tajkhorshid, E.,  Neutze, R.,  Kjellbom, P.

Journal: (2006) Nature 439: 688-694

PubMed: 16340961  
DOI: 10.1038/nature04316  
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PubMed Abstract:
Plants counteract fluctuations in water supply by regulating all aquaporins in the cell plasma membrane. Channel closure results either from the dephosphorylation of two conserved serine residues under conditions of drought stress, or from the protonation of a conserved histidine... [ Read More & Search PubMed Abstracts ]
 
  •   Molecular Description Hide
    Classification: Transport Protein , Membrane Protein
    Structure Weight: 130179.60
    Molecule: aquaporin
    Polymer: 1 Type: protein Length: 303
    Chains: A, B, C, D
    Organism Spinacia oleracea
    UniProtKB:   Protein Feature View | Search PDB | Q41372  
    Q41372UniProtKBSecstruc2B5F.A2B5F.D2B5F.C2B5F.BPDBTooltip
     
  •   Source Hide
    Polymer: 1
    Scientific Name: Spinacia oleracea   Taxonomy   Common Name: Spinach Expression System: Pichia pastoris  
     
  •   Related PDB Entries Hide
    Identifier Details
    1Z98  The same protein in a closed conformation to high resolution 
     
  •   External Domain Annotations Hide
     
  •   Structural Biology Knowledgebase Data Hide

    Information from the Structural Biology Knowledgebase  

     
 
Data in orange boxes are gathered from external resources (when available).
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  Biological Assembly       
Biological assembly 1 assigned by authors and generated by PISA (software)
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