2IUB
Crystal structure of a divalent metal ion transporter CorA at 2.9 A resolution.
Summary for 2IUB
Entry DOI | 10.2210/pdb2iub/pdb |
Related | 2BBH 2BBJ |
Descriptor | DIVALENT CATION TRANSPORT-RELATED PROTEIN, CHLORIDE ION, MAGNESIUM ION, ... (4 entities in total) |
Functional Keywords | membrane protein, cora, divalent cation, ion transporter |
Biological source | THERMOTOGA MARITIMA |
Cellular location | Cell inner membrane; Multi-pass membrane protein: Q9WZ31 |
Total number of polymer chains | 10 |
Total formula weight | 430355.61 |
Authors | Eshaghi, S.,Niegowski, D.,Kohl, A.,Martinez Molina, D.,Lesley, S.A.,Nordlund, P. (deposition date: 2006-06-01, release date: 2006-08-03, Last modification date: 2024-05-08) |
Primary citation | Eshaghi, S.,Niegowski, D.,Kohl, A.,Martinez Molina, D.,Lesley, S.A.,Nordlund, P. Crystal Structure of a Divalent Metal Ion Transporter Cora at 2.9 Angstrom Resolution. Science, 313:354-, 2006 Cited by PubMed Abstract: CorA family members are ubiquitously distributed transporters of divalent metal cations and are considered to be the primary Mg2+ transporter of Bacteria and Archaea. We have determined a 2.9 angstrom resolution structure of CorA from Thermotoga maritima that reveals a pentameric cone-shaped protein. Two potential regulatory metal binding sites are found in the N-terminal domain that bind both Mg2+ and Co2+. The structure of CorA supports an efflux system involving dehydration and rehydration of divalent metal ions potentially mediated by a ring of conserved aspartate residues at the cytoplasmic entrance and a carbonyl funnel at the periplasmic side of the pore. PubMed: 16857941DOI: 10.1126/SCIENCE.1127121 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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