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6F2W

Bacterial asc transporter crystal structure in open to in conformation

Summary for 6F2W
Entry DOI10.2210/pdb6f2w/pdb
Related6F2G
DescriptorPutative amino acid/polyamine transport protein, Nanobody 74, ALPHA-AMINOISOBUTYRIC ACID, ... (4 entities in total)
Functional Keywordsleut fold, lat transporter, apc transporter, transport protein
Biological sourceCarnobacterium sp. AT7
More
Total number of polymer chains2
Total formula weight62188.92
Authors
Fort, J.,Errasti-Murugarren, E.,Carpena, X.,Palacin, M.,Fita, I. (deposition date: 2017-11-27, release date: 2019-04-24, Last modification date: 2024-01-17)
Primary citationErrasti-Murugarren, E.,Fort, J.,Bartoccioni, P.,Diaz, L.,Pardon, E.,Carpena, X.,Espino-Guarch, M.,Zorzano, A.,Ziegler, C.,Steyaert, J.,Fernandez-Recio, J.,Fita, I.,Palacin, M.
L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction.
Nat Commun, 10:1807-1807, 2019
Cited by
PubMed Abstract: L-amino acid transporters (LATs) play key roles in human physiology and are implicated in several human pathologies. LATs are asymmetric amino acid exchangers where the low apparent affinity cytoplasmic side controls the exchange of substrates with high apparent affinity on the extracellular side. Here, we report the crystal structures of an LAT, the bacterial alanine-serine-cysteine exchanger (BasC), in a non-occluded inward-facing conformation in both apo and substrate-bound states. We crystallized BasC in complex with a nanobody, which blocks the transporter from the intracellular side, thus unveiling the sidedness of the substrate interaction of BasC. Two conserved residues in human LATs, Tyr 236 and Lys 154, are located in equivalent positions to the Na1 and Na2 sites of sodium-dependent APC superfamily transporters. Functional studies and molecular dynamics (MD) calculations reveal that these residues are key for the asymmetric substrate interaction of BasC and in the homologous human transporter Asc-1.
PubMed: 31000719
DOI: 10.1038/s41467-019-09837-z
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.4 Å)
Structure validation

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