Crystal Structure of a Divalent Metal Ion Transporter Cora at 2.9 Angstrom Resolution.
From: Division of Biophysics, Department of Medical Biochemistry and Biophysics, Karolinska Institute, SE-171 77 Stockholm, Sweden. Said.Eshaghi@ki.se
Science (New York, N.Y.)
- Publish Date: Jul 2006
- ISSN: 1095-9203
- Volume: 313
- Issue: 5785
- Pages: 354-7
- Medium: Internet
- Language: English
- Citation (JAMA): Eshaghi Said, Niegowski Damian, Kohl Andreas, et al. Crystal Structure of a Divalent Metal Ion Transporter Cora at 2.9 Angstrom Resolution.. Science Jul 2006;313:354-7
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.
Mesh Headings (Keywords): Amino Acid Sequence, Bacterial Proteins, Binding Sites, Cation Transport Proteins, Chlorides, Cobalt, Crystallography, X-Ray, Hydrophobicity, Magnesium, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Folding, Protein Structure, Quaternary, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Alignment, Thermotoga maritima, Water
Check for Full Text / PubMed Unique Identifier (PMID): 16857941
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