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

• 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.

Subject headings

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)

NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

Keyword

Magnesium

cora

transporter

channel

membrane proteins

Biochemistry

Biokemi

strukturbiologi

Structural Biology

Publication and Content Type

ref (subject category)

art (subject category)