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Crystal Structure of a Divalent Metal Ion Transporter CorA at 2.9 Angstrom Resolution

Science  21 Jul 2006:
Vol. 313, Issue 5785, pp. 354-357
DOI: 10.1126/science.1127121

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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.

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