Extended Data Fig. 2: Sequence alignment of Mrs2 and CorA proteins. | Nature Structural & Molecular Biology

Extended Data Fig. 2: Sequence alignment of Mrs2 and CorA proteins.

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

Extended Data Fig. 2

The following sequences are included in the alignment (Uniprot-ID in brackets): CtMrs2 from Chaetomium thermophilum (G0S186), ScMrs2 from Saccharomyces cerevisiae (Q01926), HsMrs2 (or hMrs2) from Homo sapiens (Q9HD23), MmMrs2 from Mus musculus (Mouse) (Q5NCE8), DrMrs2 from Danio rerio (E7F680), TmCorA from Thermotoga maritima (Q9WZ31) and MjCorA from Methanocaldococcus jannaschii (Q58439). There is relatively low sequence homology between Mrs2 and CorA proteins (for example 35 % between TmCorA and the equivalent from Saccharomyces cerevisiae, ScMrs2) and even among Mrs2 members (for example 47 % between ScMrs2 and hMrs2). α-helices and β-strands are labelled with black arrows and grey cylinders as derived using the CtMrs2 structure. Black and blue arrowheads mark residues involved in gating (conserved arginine among Mrs2 proteins are highlighted with dark green box) and in Mg2+-binding, respectively. Green boxes denote the conserved GMN-motif selectivity filter and the conserved RDLR-regulation motif. Red circles represent residues of the conserved acidic loop. Wheat boxes show TM1 and TM2. Sequence alignments were performed using Cluster Omega (online) and visualized using ESPript 3.0 (online).

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