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Science 21 July 2006:
Vol. 313. no. 5785, pp. 354 - 357
DOI: 10.1126/science.1127121
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Reports

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

Said Eshaghi,1*{dagger} Damian Niegowski,1,2* Andreas Kohl,1 Daniel Martinez Molina,1,2 Scott A. Lesley,3 Pär Nordlund1{dagger}

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.

1 Division of Biophysics, Department of Medical Biochemistry and Biophysics, Karolinska Institute, SE-171 77 Stockholm, Sweden.
2 Department of Biochemistry and Biophysics, Stockholm University, S-106 91 Stockholm, Sweden.
3 Joint Center for Structural Genomics and Genomics Institute of the Novartis Research Foundation, San Diego, CA 92121, USA.

* These authors contributed equally to this work.

{dagger} To whom correspondence should be addressed. E-mail: Par.Nordlund{at}ki.se (P.N.); Said.Eshaghi{at}ki.se (S.E.)

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