5EZB

Chicken prestin STAS domain

Summary for 5EZB

• Entry DOI: 10.2210/pdb5ezb/pdb
• Related: 3LLO 5EUS 5EUU 5EUW 5EUX 5EUZ
• Descriptor: Chicken prestin STAS domain,Chicken prestin STAS domain, ZINC ION, GLYCEROL, ... (6 entities in total)
• Functional Keywords: eukaryotic slc26 stas fold, transport protein
• Biological source: Gallus gallus (Chicken); More
• Cellular location: Membrane ; Multi-pass membrane protein : A0FKN5
• Total number of polymer chains: 2
• Total formula weight: 32298.02

Authors

Lolli, G.,Pasqualetto, E.,Costanzi, E.,Bonetto, G.,Battistutta, R. (deposition date: 2015-11-26, release date: 2015-12-16, Last modification date: 2024-01-10)

Primary citation

Lolli, G.,Pasqualetto, E.,Costanzi, E.,Bonetto, G.,Battistutta, R.
The STAS domain of mammalian SLC26A5 prestin harbours an anion-binding site.
Biochem.J., 473:365-370, 2016

PubMed Abstract: 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.

PubMed: 26635354
DOI: 10.1042/BJ20151089

Experimental method

X-RAY DIFFRACTION (2.3 Å)