期刊
BIOCHEMICAL JOURNAL
卷 473, 期 -, 页码 365-370出版社
PORTLAND PRESS LTD
DOI: 10.1042/BJ20151089
关键词
anion transporters; crystal structure; electromotility; prestin; SLC26; STAS domain
资金
- European Community's Seventh Framework Programme (FP7) under BioStruct-X [283570]
- Fondazione Cassa di Risparmio di Padova e Rovigo
Prestin is a unique ATP- and Ca2+-independent molecular motor with piezoelectric characteristics responsible for the electromotile properties of mammalian cochlear outer hair cells, i.e. the capacity of these cells to modify their length in response to electric stimuli. This 'electromotility' is at the basis of the exceptional sensitivity and frequency selectivity distinctive of mammals. Prestin belongs to the SLC26 (solute carrier 26) family of anion transporters and needs anions to function properly, particularly Cl-. In the present study, using X-ray crystallography we reveal that the STAS (sulfate transporter and anti-sigma factor antagonist) domain of mammalian prestin, considered an 'incomplete' transporter, harbours an unanticipated anion-binding site. In parallel, we present the first crystal structure of a prestin STAS domain from a non-mammalian vertebrate prestin (chicken) that behaves as a 'full' transporter. Notably, in chicken STAS, the anion-binding site is lacking because of a local structural rearrangement, indicating that the presence of the STAS anion-binding site is exclusive to mammalian prestin.
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