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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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PDB id:
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Transport protein
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Title:
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Rat prestin stas domain in complex with thiocyanate
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Structure:
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Prestin,prestin. Chain: a. Fragment: stas domain,stas domain. Synonym: solute carrier family 26 member 5,solute carrier family 26 member 5. Engineered: yes. Mutation: yes. Other_details: residues 564-636 (variable loop) are deleted, glyser are inserted between position 563 and 637
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Source:
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Rattus norvegicus. Norway rat. Organism_taxid: 10116. Gene: slc26a5, pres. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Resolution:
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2.04Å
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R-factor:
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0.165
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R-free:
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0.198
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Authors:
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G.Lolli,E.Pasqualetto,E.Costanzi,G.Bonetto,R.Battistutta
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Key ref:
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G.Lolli
et al.
(2016).
The STAS domain of mammalian SLC26A5 prestin harbours an anion-binding site.
Biochem J,
473,
365-370.
PubMed id:
DOI:
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Date:
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19-Nov-15
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Release date:
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16-Dec-15
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PROCHECK
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Headers
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References
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Q9EPH0
(S26A5_RAT) -
Prestin from Rattus norvegicus
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Seq:
Struc:
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744 a.a.
129 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Biochem J
473:365-370
(2016)
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PubMed id:
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The STAS domain of mammalian SLC26A5 prestin harbours an anion-binding site.
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G.Lolli,
E.Pasqualetto,
E.Costanzi,
G.Bonetto,
R.Battistutta.
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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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