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Crystal structure of a divalent metal ion transporter CorA at 2.9 angstrom resolution

, : Crystal structure of a divalent metal ion transporter CorA at 2.9 angstrom resolution. Science 313(5785): 354-357

CorA family members are ubiquitously distributed transporters of divalent metal cations and are considered to be the primary Mg superscript 2+(B 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 Mg superscript 2+(B and Co superscript 2+(B. 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.


PMID: 16857941

DOI: 10.1126/science.1127121

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