1LNQ

CRYSTAL STRUCTURE OF MTHK AT 3.3 A


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.30 Å
  • R-Value Free: 0.318 
  • R-Value Work: 0.301 
  • R-Value Observed: 0.301 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

CRYSTAL STRUCTURE AND MECHANISM OF A CALCIUM-GATED POTASSIUM CHANNEL

JIANG, Y.LEE, A.CHEN, J.CADENE, M.CHAIT, B.T.MACKINNON, R.

(2002) Nature 417: 515-522

  • DOI: https://doi.org/10.1038/417515a
  • Primary Citation of Related Structures:  
    1LNQ

  • PubMed Abstract: 

    Ion channels exhibit two essential biophysical properties; that is, selective ion conduction, and the ability to gate-open in response to an appropriate stimulus. Two general categories of ion channel gating are defined by the initiating stimulus: ligand binding (neurotransmitter- or second-messenger-gated channels) or membrane voltage (voltage-gated channels). Here we present the structural basis of ligand gating in a K(+) channel that opens in response to intracellular Ca(2+). We have cloned, expressed, analysed electrical properties, and determined the crystal structure of a K(+) channel (MthK) from Methanobacterium thermoautotrophicum in the Ca(2+)-bound, opened state. Eight RCK domains (regulators of K(+) conductance) form a gating ring at the intracellular membrane surface. The gating ring uses the free energy of Ca(2+) binding in a simple manner to perform mechanical work to open the pore.


  • Organizational Affiliation

    Howard Hughes Medical Institute, Laboratory of Molecular Neurobiology and Biophysics, Rockefeller University, 1230 York Avenue, New York, New York 10021, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
POTASSIUM CHANNEL RELATED PROTEIN
A, B, C, D, E
A, B, C, D, E, F, G, H
336Methanothermobacter thermautotrophicusMutation(s): 0 
Gene Names: mth1520
Membrane Entity: Yes 
UniProt
Find proteins for O27564 (Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H))
Explore O27564 
Go to UniProtKB:  O27564
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO27564
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.30 Å
  • R-Value Free: 0.318 
  • R-Value Work: 0.301 
  • R-Value Observed: 0.301 
  • Space Group: P 61
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 137α = 90
b = 137β = 90
c = 373.3γ = 120
Software Package:
Software NamePurpose
SHARPphasing
MLPHAREphasing
CNSrefinement
HKL-2000data reduction
SCALEPACKdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2002-06-19
    Type: Initial release
  • Version 1.1: 2007-10-16
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2014-11-12
    Changes: Structure summary
  • Version 1.4: 2024-02-14
    Changes: Data collection, Database references, Derived calculations