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Membrane protein PDB id
1bl8
Jmol
Contents
Protein chains
97 a.a. *
Metals
__K ×3
Waters ×1
* Residue conservation analysis
PDB id:
1bl8
Name: Membrane protein
Title: Potassium channel (kcsa) from streptomyces lividans
Structure: Protein (potassium channel protein). Chain: a, b, c, d. Engineered: yes. Mutation: yes
Source: Streptomyces lividans. Organism_taxid: 1916. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Tetramer (from PQS)
Resolution:
3.20Å     R-factor:   0.280     R-free:   0.290
Authors: D.A.Doyle,J.M.Cabral,R.A.Pfuetzner,A.Kuo,J.M.Gulbis,S.L.Cohe B.T.Chait,R.Mackinnon
Key ref:
D.A.Doyle et al. (1998). The structure of the potassium channel: molecular basis of K+ conduction and selectivity. Science, 280, 69-77. PubMed id: 9525859 DOI: 10.1126/science.280.5360.69
Date:
23-Jul-98     Release date:   29-Jul-98    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0A334  (KCSA_STRLI) -  Voltage-gated potassium channel
Seq:
Struc: 		160 a.a.
97 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     voltage-gated potassium channel complex   1 term 
  Biological process     potassium ion transport   1 term 
  Biochemical function     voltage-gated potassium channel activity     1 term  

 

 
DOI no: 10.1126/science.280.5360.69 Science 280:69-77 (1998)
PubMed id: 9525859  
 
 
The structure of the potassium channel: molecular basis of K+ conduction and selectivity.
D.A.Doyle, J.Morais Cabral, R.A.Pfuetzner, A.Kuo, J.M.Gulbis, S.L.Cohen, B.T.Chait, R.MacKinnon.
 
  ABSTRACT  
 
The potassium channel from Streptomyces lividans is an integral membrane protein with sequence similarity to all known K+ channels, particularly in the pore region. X-ray analysis with data to 3.2 angstroms reveals that four identical subunits create an inverted teepee, or cone, cradling the selectivity filter of the pore in its outer end. The narrow selectivity filter is only 12 angstroms long, whereas the remainder of the pore is wider and lined with hydrophobic amino acids. A large water-filled cavity and helix dipoles are positioned so as to overcome electrostatic destabilization of an ion in the pore at the center of the bilayer. Main chain carbonyl oxygen atoms from the K+ channel signature sequence line the selectivity filter, which is held open by structural constraints to coordinate K+ ions but not smaller Na+ ions. The selectivity filter contains two K+ ions about 7.5 angstroms apart. This configuration promotes ion conduction by exploiting electrostatic repulsive forces to overcome attractive forces between K+ ions and the selectivity filter. The architecture of the pore establishes the physical principles underlying selective K+ conduction.
 
  Selected figure(s)  
 
Figure 6.
Fig. 6. Identification of permeant ion positions in the pore. (a) A Rb^+ difference Fourier map calculated to 4.0 Å and contoured at 6^ identifies two strong peaks corresponding to ions in the selectivity filter (inner and outer ions) and a weaker peak corresponding to ions in the cavity (cavity ion). The inner ion density has two closely spaced peaks. (b) A Cs+ difference Fourier map calculated to 5.0 Å and contoured at 6^ shows the inner and outer ion peaks in the selectivity filter. Both difference Fourier maps were calculated with Fourier coefficients: F(soak) - F(native-unsharpened) and MIR phases. (c) Electron density map contoured at 1 showing diffuse density at the cavity ion position. This map was calculated with the following Fourier coefficients: unsharpened native amplitudes and MIR solvent-flattened^ phases (no averaging information was included). 		Figure 7.
Fig. 7. Two mechanisms by which the K+ channel stabilizes a cation in the middle of the membrane. First, a large aqueous cavity stabilizes an ion (green) in the otherwise hydrophobic membrane interior. Second, oriented helices point their partial negative charge (carboxyl end, red) towards the cavity where a cation is located.
 
  The above figures are reprinted by permission from the AAAs: Science (1998, 280, 69-77) copyright 1998.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

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