5EUS

Rat prestin STAS domain in complex with bromide

Summary for 5EUS

• Entry DOI: 10.2210/pdb5eus/pdb
• Related: 3LLO
• Descriptor: Prestin,Rat prestin STAS domain, BROMIDE ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• Functional Keywords: anion-binding site, protein-anion complex, transport protein
• Biological source: Rattus norvegicus (Norway Rat); More
• Cellular location: Cell membrane; Multi-pass membrane protein: Q9EPH0
• Total number of polymer chains: 1
• Total formula weight: 16289.11

Authors

Lolli, G.,Pasqualetto, E.,Costanzi, E.,Bonetto, G.,Battistutta, R. (deposition date: 2015-11-19, 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 (1.833 Å)