4egw

The structure of the soluble domain of CorA from Methanocaldococcus jannaschii

spinqualitylabelsall models 4egw, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4egw is a 2 chain structure with sequence from Methanocaldococcus jannaschii DSM 2661. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BU1, HEZ, MG, PGO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CORA_METJA] Mediates influx of magnesium ions. Publication Abstract from PubMed Despite the importance of Mg(2+) for numerous cellular activities, the mechanisms underlying its import and homeostasis are poorly understood. The CorA family is ubiquitous and is primarily responsible for Mg(2+) transport. However, the key questions-such as, the ion selectivity, the transport pathway, and the gating mechanism-have remained unanswered for this protein family. We present a 3.2 A resolution structure of the archaeal CorA from Methanocaldococcus jannaschii, which is a unique complete structure of a CorA protein and reveals the organization of the selectivity filter, which is composed of the signature motif of this family. The structure reveals that polar residues facing the channel coordinate a partially hydrated Mg(2+) during the transport. Based on these findings, we propose a unique gating mechanism involving a helical turn upon the binding of Mg(2+) to the regulatory intracellular binding sites, and thus converting a polar ion passage into a narrow hydrophobic pore. Because the amino acids involved in the uptake, transport, and gating are all conserved within the entire CorA family, we believe this mechanism is general for the whole family including the eukaryotic homologs. Structural insights into the mechanisms of Mg2+ uptake, transport, and gating by CorA.,Guskov A, Nordin N, Reynaud A, Engman H, Lundback AK, Jong AJ, Cornvik T, Phua T, Eshaghi S Proc Natl Acad Sci U S A. 2012 Nov 6;109(45):18459-64. doi:, 10.1073/pnas.1210076109. Epub 2012 Oct 22. PMID:23091000 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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