5ezb | pdb_00005ezb

Chicken prestin STAS domain

spinqualitylabelsall models 5ezb, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ezb is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, NA, OXL, ZN Related: 3llo, 5eus, 5euu, 5euw, 5eux, 5euz Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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