Document Detail


Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing.
MedLine Citation:
PMID:  23033078     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Voltage-gated sodium channels are vital membrane proteins essential for electrical signalling; in humans, they are key targets for the development of pharmaceutical drugs. Here we report the crystal structure of an open-channel conformation of NavMs, the bacterial channel pore from the marine bacterium Magnetococcus sp. (strain MC-1). It differs from the recently published crystal structure of a closed form of a related bacterial sodium channel (NavAb) by having its internal cavity accessible to the cytoplasmic surface as a result of a bend/rotation about a central residue in the carboxy-terminal transmembrane segment. This produces an open activation gate of sufficient diameter to allow hydrated sodium ions to pass through. Comparison of the open and closed structures provides new insight into the features of the functional states present in the activation cycles of sodium channels and the mechanism of channel opening and closing.
Authors:
Emily C McCusker; Claire Bagnéris; Claire E Naylor; Ambrose R Cole; Nazzareno D'Avanzo; Colin G Nichols; B A Wallace
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Nature communications     Volume:  3     ISSN:  2041-1723     ISO Abbreviation:  Nat Commun     Publication Date:  2012  
Date Detail:
Created Date:  2012-10-03     Completed Date:  2013-02-01     Revised Date:  2014-03-19    
Medline Journal Info:
Nlm Unique ID:  101528555     Medline TA:  Nat Commun     Country:  England    
Other Details:
Languages:  eng     Pagination:  1102     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Bacterial Proteins / chemistry*,  metabolism*
Circular Dichroism
Molecular Sequence Data
Protein Structure, Secondary
Protein Structure, Tertiary
Structure-Activity Relationship
Voltage-Gated Sodium Channels / chemistry*,  metabolism*
Grant Support
ID/Acronym/Agency:
HL54171/HL/NHLBI NIH HHS; R01 HL054171/HL/NHLBI NIH HHS; //Biotechnology and Biological Sciences Research Council
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Voltage-Gated Sodium Channels
Comments/Corrections

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