3GI8
Crystal Structure of ApcT K158A Transporter Bound to 7F11 Monoclonal Fab Fragment
Summary for 3GI8
| Entry DOI | 10.2210/pdb3gi8/pdb |
| Related | 3GI9 3GIA |
| Descriptor | Uncharacterized protein MJ0609, 7F11 Anti-ApcT Monoclonal Fab Light Chain, 7F11 Anti-ApcT Monoclonal Fab Heavy Chain, ... (4 entities in total) |
| Functional Keywords | membrane protein, transporter, antibody, 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) More |
| Cellular location | Cell membrane; Multi-pass membrane protein (Potential): Q58026 |
| Total number of polymer chains | 3 |
| Total formula weight | 96541.62 |
| 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: 2024-11-20) |
| 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 Cited by 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: 19608859DOI: 10.1126/science.1176088 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.59 Å) |
Structure validation
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