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The Formate/Nitrite Transporter Family Of Anion Channels.
MedLine Citation:
PMID:  23380538     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Abstract The Formate/Nitrite Transporter family of integral membrane proteins comprises pentameric channels for monovalent anions that exhibit a broad specificity for small anions such as chlo-ride, the physiological cargo molecules formate, nitrite and hydrosulfide, and also larger or-ganic acids. Three-dimensional structures are available for the three known subtypes, FocA, NirC, and HSC that reveal remarkable evolutionary optimizations for the respective physio-logical context of the channels. FNT channels share a conserved translocation pathway in each protomer, with a central hydrophobic cavity that is separated from both sides of the membrane by a narrow constriction. A single protonable residue, a histidine, plays a key role by tran-siently protonating the transported anion to allow an uncharged species to pass the hydrophobic barrier. Further selectivity is reached through variations in the electrostatic surface potential of the proteins, priming the formate channel FocA for anion export, while NirC and HSC should work bidirectionally. Electrophysiological studies have shown that a broad variety of monova-lent anions can be transported, and in the case of FocA these match exactly the products of mixed-acid fermentation, the predominant metabolic pathway for most enterobacterial species.
Authors:
Wei Lü; Juan Du; Nikola J Schwarzer; Tobias Wacker; Susana L A Andrade; Oliver Einsle
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-2-6
Journal Detail:
Title:  Biological chemistry     Volume:  -     ISSN:  1437-4315     ISO Abbreviation:  Biol. Chem.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-2-5     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9700112     Medline TA:  Biol Chem     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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