Chicken prestin STAS domainChicken prestin STAS domain

Structural highlights

5ezb is a 2 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0FKN5_CHICK

Publication Abstract from PubMed

Prestin is a unique ATP- and Ca2+-independent molecular motor with piezoelectric characteristic responsible for the electromotile properties of mammalian cochlear outer hair cells, that is 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 family of anion transporters and needs anions to function properly, in particular chloride. By X-ray crystallography here we reveal that the STAS domain of mammalian prestin, considered an "incomplete" transporter, harbor 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 due to a local structural rearrangement, indicating that the presence of the STAS anion-binding site is exclusive to mammalian prestin.

The STAS domain of mammalian SLC26A5 prestin harbors an anion-binding site.,Lolli G, Pasqualetto E, Costanzi E, Bonetto G, Battistutta R Biochem J. 2015 Dec 3. pii: BJ20151089. PMID:26635354[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Lolli G, Pasqualetto E, Costanzi E, Bonetto G, Battistutta R. The STAS domain of mammalian SLC26A5 prestin harbors an anion-binding site. Biochem J. 2015 Dec 3. pii: BJ20151089. PMID:26635354 doi:http://dx.doi.org/10.1042/BJ20151089

5ezb, resolution 2.30Å

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