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PDBsum entry 2wlk
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protein ligands metals Protein-protein interface(s) links
Metal transport PDB id
2wlk

 

 

 

 

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Contents
Protein chains
291 a.a. *
Ligands
SPM
Metals
__K ×5
_CL
Waters ×33
* Residue conservation analysis
PDB id:
2wlk
Name: Metal transport
Title: Structure of the atp-sensitive inward rectifier potassium channel from magnetospirillum magnetotacticum
Structure: Atp-sensitive inward rectifier potassium channel 10. Chain: a, b. Synonym: kirbac3.1. Engineered: yes
Source: Magnetospirillum magnetotacticum. Organism_taxid: 188. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.80Å     R-factor:   0.248     R-free:   0.280
Authors: O.B.Clarke,A.T.Caputo,B.J.Smith,J.M.Gulbis
Key ref: O.B.Clarke et al. (2010). Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels. Cell, 141, 1018-1029. PubMed id: 20564790
Date:
24-Jun-09     Release date:   09-Jun-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
D9N164  (IRK10_PARME) -  Inward rectifier potassium channel Kirbac3.1 from Paramagnetospirillum magnetotacticum
Seq:
Struc: 		295 a.a.
291 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Cell 141:1018-1029 (2010)
PubMed id: 20564790  
 
 
Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels.
O.B.Clarke, A.T.Caputo, A.P.Hill, J.I.Vandenberg, B.J.Smith, J.M.Gulbis.
 
  ABSTRACT  
 
Potassium channels embedded in cell membranes employ gates to regulate K+ current. While a specific constriction in the permeation pathway has historically been implicated in gating, recent reports suggest that the signature ion selectivity filter located in the outer membrane leaflet may be equally important. Inwardly rectifying K+ channels also control the directionality of flow, using intracellular polyamines to stem ion efflux by a valve-like action. This study presents crystallographic evidence of interdependent gates in the conduction pathway and reveals the mechanism of polyamine block. Reorientation of the intracellular domains, concomitant with activation, instigates polyamine release from intracellular binding sites to block the permeation pathway. Conformational adjustments of the slide helices, achieved by rotation of the cytoplasmic assembly relative to the pore, are directly correlated to the ion configuration in the selectivity filter. Ion redistribution occurs irrespective of the constriction, suggesting a more expansive role of the selectivity filter in gating than previously appreciated.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
22231399 V.N.Bavro, R.De Zorzi, M.R.Schmidt, J.R.Muniz, L.Zubcevic, M.S.Sansom, C.Vénien-Bryan, and S.J.Tucker (2012).
Structure of a KirBac potassium channel with an open bundle crossing indicates a mechanism of channel gating.
  Nat Struct Mol Biol, 19, 158-163.
PDB code: 3zrs
21170050 D.T.Wang, A.P.Hill, S.A.Mann, P.S.Tan, and J.I.Vandenberg (2011).
Mapping the sequence of conformational changes underlying selectivity filter gating in the K(v)11.1 potassium channel.
  Nat Struct Mol Biol, 18, 35-41.  
21543849 F.Gorrec, C.M.Palmer, G.Lebon, and T.Warne (2011).
Pi sampling: a methodical and flexible approach to initial macromolecular crystallization screening.
  Acta Crystallogr D Biol Crystallogr, 67, 463-470.  
21874019 S.B.Hansen, X.Tao, and R.MacKinnon (2011).
Structural basis of PIP2 activation of the classical inward rectifier K+ channel Kir2.2.
  Nature, 477, 495-498.
PDB codes: 3spc 3spg 3sph 3spi 3spj
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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