5oqt

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

spinqualitylabelsall models 5oqt, resolution 2.86Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5oqt is a 2 chain structure with sequence from Escherichia coli K-12 and Geobacillus kaustophilus HTA426. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.86Å Ligands: ACT, ALA, CL, CLR, OLC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5L1G5_GEOKA Publication Abstract from PubMed 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. Structural basis for amino acid transport by the CAT family of SLC7 transporters.,Jungnickel KEJ, Parker JL, Newstead S Nat Commun. 2018 Feb 7;9(1):550. doi: 10.1038/s41467-018-03066-6. PMID:29416041 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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