Structural highlights
Function
CORA_THEMA Mediates influx of magnesium ions (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Eshaghi S, Niegowski D, Kohl A, Martinez Molina D, Lesley SA, Nordlund P. Crystal structure of a divalent metal ion transporter CorA at 2.9 angstrom resolution. Science. 2006 Jul 21;313(5785):354-7. PMID:16857941 doi:http://dx.doi.org/313/5785/354
