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PDBsum entry 4zzc

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protein ligands metals Protein-protein interface(s) links
Membrane protein, transport protein PDB id
4zzc

 

 

 

 

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Contents
Protein chains
311 a.a.
Ligands
ACT ×10
PLC ×10
LMT ×6
_XE ×30
Metals
_CL ×5
_NA ×6
Waters ×7
PDB id:
4zzc
Name: Membrane protein, transport protein
Title: The glic pentameric ligand-gated ion channel open form complexed to xenon
Structure: Proton-gated ion channel. Chain: a, b, c, d, e. Synonym: glic,ligand-gated ion channel,lgic, glic pentameric ligand- gated ion channel. Engineered: yes
Source: Gloeobacter violaceus (strain pcc 7421). Organism_taxid: 251221. Strain: pcc 7421. Gene: glvi, glr4197. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
3.10Å     R-factor:   0.209     R-free:   0.228
Authors: L.Sauguet,Z.Fourati,T.Prange,M.Delarue,N.Colloc'H
Key ref: L.Sauguet et al. (2016). Structural Basis for Xenon Inhibition in a Cationic Pentameric Ligand-Gated Ion Channel. Plos One, 11, e0149795. PubMed id: 26910105 DOI: 10.1371/journal.pone.0149795
Date:
22-May-15     Release date:   02-Mar-16    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q7NDN8  (GLIC_GLOVI) -  Proton-gated ion channel from Gloeobacter violaceus (strain ATCC 29082 / PCC 7421)
Seq:
Struc:
359 a.a.
311 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1371/journal.pone.0149795 Plos One 11:e0149795 (2016)
PubMed id: 26910105  
 
 
Structural Basis for Xenon Inhibition in a Cationic Pentameric Ligand-Gated Ion Channel.
L.Sauguet, Z.Fourati, T.Prangé, M.Delarue, N.Colloc'h.
 
  ABSTRACT  
 
GLIC receptor is a bacterial pentameric ligand-gated ion channel whose action is inhibited by xenon. Xenon has been used in clinical practice as a potent gaseous anaesthetic for decades, but the molecular mechanism of interactions with its integral membrane receptor targets remains poorly understood. Here we characterize by X-ray crystallography the xenon-binding sites within both the open and "locally-closed" (inactive) conformations of GLIC. Major binding sites of xenon, which differ between the two conformations, were identified in three distinct regions that all belong to the trans-membrane domain of GLIC: 1) in an intra-subunit cavity, 2) at the interface between adjacent subunits, and 3) in the pore. The pore site is unique to the locally-closed form where the binding of xenon effectively seals the channel. A putative mechanism of the inhibition of GLIC by xenon is proposed, which might be extended to other pentameric cationic ligand-gated ion channels.
 

 

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