3OR6

On the structural basis of modal gating behavior in K+channels - E71Q


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.268 
  • R-Value Work: 0.226 

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This is version 1.2 of the entry. See complete history


Literature

On the structural basis of modal gating behavior in K(+) channels.

Chakrapani, S.Cordero-Morales, J.F.Jogini, V.Pan, A.C.Cortes, D.M.Roux, B.Perozo, E.

(2011) Nat Struct Mol Biol 18: 67-74

  • DOI: https://doi.org/10.1038/nsmb.1968
  • Primary Citation of Related Structures:  
    3OR6, 3OR7

  • PubMed Abstract: 

    Modal-gating shifts represent an effective regulatory mechanism by which ion channels control the extent and time course of ionic fluxes. Under steady-state conditions, the K(+) channel KcsA shows three distinct gating modes, high-P(o), low-P(o) and a high-frequency flicker mode, each with about an order of magnitude difference in their mean open times. Here we show that in the absence of C-type inactivation, mutations at the pore-helix position Glu71 unmask a series of kinetically distinct modes of gating in a side chain-specific way. These gating modes mirror those seen in wild-type channels and suggest that specific interactions in the side chain network surrounding the selectivity filter, in concert with ion occupancy, alter the relative stability of pre-existing conformational states of the pore. The present results highlight the key role of the selectivity filter in regulating modal gating behavior in K(+) channels.


  • Organizational Affiliation

    Department of Biochemistry and Molecular Biology, University of Chicago, Center for Integrative Science, Chicago, Illinois, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
antibody fab fragment heavy chain219Mus musculusMutation(s): 0 
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
antibody fab fragment light chain212Mus musculusMutation(s): 0 
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Voltage-gated potassium channel103Streptomyces lividansMutation(s): 1 
Membrane Entity: Yes 
UniProt
Find proteins for P0A334 (Streptomyces lividans)
Explore P0A334 
Go to UniProtKB:  P0A334
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UniProt GroupP0A334
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.268 
  • R-Value Work: 0.226 
  • Space Group: I 4
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 155.679α = 90
b = 155.679β = 90
c = 76.109γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
CNSrefinement
HKL-2000data reduction
HKL-2000data scaling
CNSphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-01-05
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2018-08-29
    Changes: Data collection, Source and taxonomy, Structure summary