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Fig. 5 | BMC Molecular and Cell Biology

Fig. 5

From: ECOD: identification of distant homology among multidomain and transmembrane domain proteins

Fig. 5

Structural and functional similarity between leucine-specific domain of LeuRS and rubredoxin-related zinc ribbons. a – structural alignment of leucine-specific domains of E.coli LeuRS (PDB: 4AQ7) and T.thermophilus LeuRS (PDB: 1H3N). Aligned regions colored by respective colors, unaligned regions colored by pale pink (E.coli LeuRS) and pale blue (T.thermophilus LeuRS). Structures of LeuRS leucine-specific domains of E.coli (b), T.thermophilus (c). d, e - Structures of T.thermophilus LeuRS zinc binding domains. Cα atoms of residues which take part in Zn binding are shown as spheres and colored in magenta. f - Rosetta model of leucine-specific domains of D.phosphitoxidans LeuRS. Residues which supposed to bind zinc are shown as spheres and colored in magenta. g – sequences alignment LeuRS leucine-specific domains, where E.c. - E.coli, D.p. - D.phosphitoxidans, T.t. - T.thermophilus. Residues which supposed to bind zinc are shown by magenta rectangles. Colored regions correspond to structurally aligned regions

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