5OQT

Crystal structure of a bacterial cationic amino acid transporter (CAT) homologue

Summary for 5OQT

• Entry DOI: 10.2210/pdb5oqt/pdb
• Descriptor: Amino acid transporter, Uncharacterized protein YneM, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, ... (8 entities in total)
• Functional Keywords: slc7, apc, leut fold, transport protein
• Biological source: Geobacillus kaustophilus (strain HTA426); More
• Cellular location: Cell inner membrane ; Single-pass membrane protein : A5A616
• Total number of polymer chains: 2
• Total formula weight: 59524.28

Authors

Jungnickel, K.E.J.,Newstead, S. (deposition date: 2017-08-14, release date: 2018-02-14, Last modification date: 2024-01-17)

Primary citation

Jungnickel, K.E.J.,Parker, J.L.,Newstead, S.
Structural basis for amino acid transport by the CAT family of SLC7 transporters.
Nat Commun, 9:550-550, 2018

PubMed Abstract: Amino acids play essential roles in cell biology as regulators of metabolic pathways. Arginine in particular is a major signalling molecule inside the cell, being a precursor for both l-ornithine and nitric oxide (NO) synthesis and a key regulator of the mTORC1 pathway. In mammals, cellular arginine availability is determined by members of the solute carrier (SLC) 7 family of cationic amino acid transporters. Whereas CAT-1 functions to supply cationic amino acids for cellular metabolism, CAT-2A and -2B are required for macrophage activation and play important roles in regulating inflammation. Here, we present the crystal structure of a close homologue of the mammalian CAT transporters that reveals how these proteins specifically recognise arginine. Our structural and functional data provide a model for cationic amino acid transport in mammalian cells and reveals mechanistic insights into proton-coupled, sodium-independent amino acid transport in the wider APC superfamily.

PubMed: 29416041
DOI: 10.1038/s41467-018-03066-6

Experimental method

X-RAY DIFFRACTION (2.86 Å)