3GIA

Crystal Structure of ApcT Transporter

Summary for 3GIA

• Entry DOI: 10.2210/pdb3gia/pdb
• Related: 3GI8 3GI9
• Descriptor: Uncharacterized protein MJ0609, DECANE, BICINE, ... (4 entities in total)
• Functional Keywords: membrane protein, transporter, cell membrane, membrane, transmembrane, transport protein, structural genomics, psi-2, protein structure initiative, new york consortium on membrane protein structure, nycomps
• Biological source: Methanocaldococcus jannaschii (Methanococcus jannaschii)
• Cellular location: Cell membrane; Multi-pass membrane protein (Potential): Q58026
• Total number of polymer chains: 1
• Total formula weight: 49347.08

Authors

Shaffer, P.L.,Goehring, A.S.,Shankaranarayanan, A.,Gouaux, E.,New York Consortium on Membrane Protein Structure (NYCOMPS) (deposition date: 2009-03-05, release date: 2009-08-18, Last modification date: 2024-04-03)

Primary citation

Shaffer, P.L.,Goehring, A.,Shankaranarayanan, A.,Gouaux, E.
Structure and mechanism of a na+-independent amino Acid transporter.
Science, 325:1010-1014, 2009

PubMed Abstract: Amino acid, polyamine, and organocation (APC) transporters are secondary transporters that play essential roles in nutrient uptake, neurotransmitter recycling, ionic homeostasis, and regulation of cell volume. Here, we present the crystal structure of apo-ApcT, a proton-coupled broad-specificity amino acid transporter, at 2.35 angstrom resolution. The structure contains 12 transmembrane helices, with the first 10 consisting of an inverted structural repeat of 5 transmembrane helices like the leucine transporter LeuT. The ApcT structure reveals an inward-facing, apo state and an amine moiety of lysine-158 located in a position equivalent to the sodium ion site Na2 of LeuT. We propose that lysine-158 is central to proton-coupled transport and that the amine group serves the same functional role as the Na2 ion in LeuT, thus demonstrating common principles among proton- and sodium-coupled transporters.

PubMed: 19608859
DOI: 10.1126/science.1176088

Experimental method

X-RAY DIFFRACTION (2.32 Å)