6LI9

Heteromeric amino acid transporter b0,+AT-rBAT complex bound with Arginine

Summary for 6LI9

• Entry DOI: 10.2210/pdb6li9/pdb
• EMDB information: 0903
• Descriptor: Neutral and basic amino acid transport protein rBAT, b(0,+)-type amino acid transporter 1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: transporter, membrane protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 280189.96

Authors

Yan, R.H.,Li, Y.N.,Lei, J.L.,Zhou, Q. (deposition date: 2019-12-10, release date: 2020-04-29, Last modification date: 2024-10-23)

Primary citation

Yan, R.,Li, Y.,Shi, Y.,Zhou, J.,Lei, J.,Huang, J.,Zhou, Q.
Cryo-EM structure of the human heteromeric amino acid transporter b0,+AT-rBAT.
Sci Adv, 6:eaay6379-eaay6379, 2020

PubMed 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 bAT (SLC7A9) is a representative light chain of HATs, forming heterodimer with rBAT, a heavy chain which mediates the membrane trafficking of bAT. The bAT-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 bAT-rBAT complex alone and in complex with arginine substrate at resolution of 2.7 and 2.3 Å, respectively. The overall structure of bAT-rBAT exists as a dimer of heterodimer consistent with the previous study. A ligand molecule is bound to the substrate binding pocket, near which an occluded pocket is identified, to which we found that it is important for substrate transport.

PubMed: 32494597
DOI: 10.1126/sciadv.aay6379

Experimental method

ELECTRON MICROSCOPY (2.3 Å)