Crystal structure of a divalent metal ion transporter CorA at 2.9 angstrom resolution
2006 (English)In: Science, ISSN 0036-8075, Vol. 313, no 5785, 354-357 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
2006. Vol. 313, no 5785, 354-357 p.
Magnesium, cora, transporter, channel, membrane proteins
Biochemistry and Molecular Biology
Research subject Structural Biology
IdentifiersURN: urn:nbn:se:su:diva-29989DOI: 10.1126/science.1127121OAI: oai:DiVA.org:su-29989DiVA: diva2:241101