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PDBsum entry 5eux
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Transport protein
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PDB id
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5eux
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References listed in PDB file
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Key reference
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Title
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The stas domain of mammalian slc26a5 prestin harbours an anion-Binding site.
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Authors
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G.Lolli,
E.Pasqualetto,
E.Costanzi,
G.Bonetto,
R.Battistutta.
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Ref.
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Biochem J, 2016,
473,
365-370.
[DOI no: ]
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PubMed id
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Abstract
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Prestin is a unique ATP- and Ca(2+)-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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Secondary reference #1
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Title
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Structure of the cytosolic portion of the motor protein prestin and functional role of the stas domain in slc26/sulp anion transporters.
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Authors
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E.Pasqualetto,
R.Aiello,
L.Gesiot,
G.Bonetto,
M.Bellanda,
R.Battistutta.
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Ref.
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J Mol Biol, 2010,
400,
448-462.
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PubMed id
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