2iub
From Proteopedia
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Revision as of 15:11, 30 October 2007
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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] with CL and MG as [ligands]. Structure known Active Site: AC1. 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
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