Extended Data Fig. 5: Structural comparisons of the closed CtMrs2 state with relevant conformations of ScMrs2, hMrs2, CorA, ZntB. | Nature Structural & Molecular Biology

Extended Data Fig. 5: Structural comparisons of the closed CtMrs2 state with relevant conformations of ScMrs2, hMrs2, CorA, ZntB.

From: Closed and open structures of the eukaryotic magnesium channel Mrs2 reveal the auto-ligand-gating regulation mechanism

Extended Data Fig. 5

a, Alignment of a CtMrs2 monomer (blue) with the AlphaFold model of ScMrs2 monomer (green) (downloaded from AlphaFold Protein Structure Database), including a close-view of the residues lining the Mg2+-conducting pathway and certain residues of the NTD. b, The soluble domain of CtMrs2 shows a similar fold as the one previously determined for the NTD of ScMrs2 (cyan, PDB-ID 3RKG). c, Alignments of CtMrs2 (blue) with human hMrs2 (wheat, PDB-ID 8IP3). The left panel shows an alignment of the pentamers, while the right panel displays an alignment of the monomers. d, Alignments of CtMrs2 (blue) with TmCorA (grey, PDB-ID 3JCF). The left panel shows an alignment of the pentamers, while the right panel displays an alignment of the monomers. e, Alignment of CtMrs2 (blue) with ZntB (orange, PDB-ID 5N9Y). The left panel shows an alignment of the pentamers, while the right panel displays an alignment of the monomers. f, Mg2+-binding sites (corresponding to site M3 and M4 in CtMrs2) of MjCoA (wheat, PDB-ID 4EV6), and a close-view with residues shown as sticks, and with Mg2+ shown as green spheres.

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