Summary for 3LRB
| Entry DOI | 10.2210/pdb3lrb/pdb |
| Related | 3LRC |
| Descriptor | Arginine/agmatine antiporter (1 entity in total) |
| Functional Keywords | transporter, antiporter, adic, amino-acid transport, antiport, cell inner membrane, cell membrane, membrane, transmembrane, transport, transport protein |
| Biological source | Escherichia coli |
| Cellular location | Cell inner membrane; Multi-pass membrane protein (By similarity): P60063 |
| Total number of polymer chains | 2 |
| Total formula weight | 93738.52 |
| Authors | |
| Primary citation | Gao, X.,Lu, F.,Zhou, L.,Dang, S.,Sun, L.,Li, X.,Wang, J.,Shi, Y. Structure and mechanism of an amino acid antiporter Science, 324:1565-1568, 2009 Cited by PubMed Abstract: Virulent enteric pathogens such as Escherichia coli strain O157:H7 rely on acid-resistance (AR) systems to survive the acidic environment in the stomach. A major component of AR is an arginine-dependent arginine:agmatine antiporter that expels intracellular protons. Here, we report the crystal structure of AdiC, the arginine:agmatine antiporter from E. coli O157:H7 and a member of the amino acid/polyamine/organocation (APC) superfamily of transporters at 3.6 A resolution. The overall fold is similar to that of several Na+-coupled symporters. AdiC contains 12 transmembrane segments, forms a homodimer, and exists in an outward-facing, open conformation in the crystals. A conserved, acidic pocket opens to the periplasm. Structural and biochemical analysis reveals the essential ligand-binding residues, defines the transport route, and suggests a conserved mechanism for the antiporter activity. PubMed: 19478139DOI: 10.1126/science.1173654 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.61 Å) |
Structure validation
Download full validation report
