2iub
From Proteopedia
CRYSTAL STRUCTURE OF A DIVALENT METAL ION TRANSPORTER CORA AT 2.9 A RESOLUTION.
Overview
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.
About this Structure
2IUB is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
Crystal structure of a divalent metal ion transporter CorA at 2.9 angstrom resolution., Eshaghi S, Niegowski D, Kohl A, Martinez Molina D, Lesley SA, Nordlund P, Science. 2006 Jul 21;313(5785):354-7. PMID:16857941 Page seeded by OCA on Sun May 4 07:53:21 2008
