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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / chemistry*
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Bacterial Proteins / metabolism
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Binding Sites
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Cation Transport Proteins / chemistry*
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Cation Transport Proteins / metabolism
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Chlorides / analysis
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Chlorides / metabolism
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Cobalt / chemistry
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Cobalt / metabolism*
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Crystallography, X-Ray
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Hydrophobic and Hydrophilic Interactions
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Magnesium / chemistry
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Magnesium / metabolism*
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Models, Molecular
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Molecular Sequence Data
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Protein Conformation
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Protein Folding
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Protein Structure, Quaternary
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Sequence Alignment
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Thermotoga maritima / chemistry*
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Water / chemistry
Substances
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Bacterial Proteins
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Cation Transport Proteins
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Chlorides
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Water
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Cobalt
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Magnesium