Cryo-EM structure of the human heteromeric amino acid transporter b^0,+AT-rBAT.

ABSTRACT: Heteromeric amino acid transporters (HATs) catalyze the transmembrane movement of amino acids, comprising two subunits, a heavy chain and a light chain, linked by a disulfide bridge. The b^0,+AT (SLC7A9) is a representative light chain of HATs, forming heterodimer with rBAT, a heavy chain which mediates the membrane trafficking of b^0,+AT. The b^0,+AT-rBAT complex is an obligatory exchanger, which mediates the influx of cystine and cationic amino acids and the efflux of neutral amino acids in kidney and small intestine. Here, we report the cryo-EM structure of the human b^0,+AT-rBAT complex alone and in complex with arginine substrate at resolution of 2.7 and 2.3 Å, respectively. The overall structure of b^0,+AT-rBAT exists as a dimer of he

SUBMITTER: Yan R 

PROVIDER: S-EPMC7159911 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature