Reaction participants Show >> << Hide
- Name help_outline L-cystine Identifier CHEBI:35491 (Beilstein: 1888247) help_outline Charge 0 Formula C6H12N2O4S2 InChIKeyhelp_outline LEVWYRKDKASIDU-IMJSIDKUSA-N SMILEShelp_outline [NH3+][C@@H](CSSC[C@H]([NH3+])C([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 14 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-leucine Identifier CHEBI:57427 Charge 0 Formula C6H13NO2 InChIKeyhelp_outline ROHFNLRQFUQHCH-YFKPBYRVSA-N SMILEShelp_outline CC(C)C[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 44 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:75043 | RHEA:75044 | RHEA:75045 | RHEA:75046 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Cryo-EM structure of the human heteromeric amino acid transporter b0,+AT-rBAT.
Yan R., Li Y., Shi Y., Zhou J., Lei J., Huang J., Zhou Q.
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<sup>0,+</sup>AT (SLC7A9) is a representative light chain of HATs, forming heterodimer with rBAT, a heavy chai ... >> More
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<sup>0,+</sup>AT (SLC7A9) is a representative light chain of HATs, forming heterodimer with rBAT, a heavy chain which mediates the membrane trafficking of b<sup>0,+</sup>AT. The b<sup>0,+</sup>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<sup>0,+</sup>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<sup>0,+</sup>AT-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. << Less
Sci. Adv. 6:eaay6379-eaay6379(2020) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.