Journal:Acta Cryst F:S2053230X20004343
From Proteopedia
Structure of Mycobacterium smegmatis α-maltose-1-phosphate synthase GlgMKarl Syson, Clare E. M. Stevenson, David M. Lawson and Stephen Bornemann [1] Molecular Tour The structure of Mycobacterium smegmatis GlgM has the expected glycosyltransferase B fold for a glycosyltransferase family 4 member. GlgM is dimeric both in solution and within the crystal. . GlgM shares many structural features with other glycosyltransferase enzymes, despite the highest sequence identity with known homologous structures being only 28%. For example, many of the amino acid side chains responsible for binding the donor substrate, ADP-glucose, are in common with members of the glycosyltransferase 5 family. These include bacterial GlgA glycogen synthases, which are absent from mycobacteria. The next step will be to see how GlgM binds glucose-1-phosphate, its acceptor substrate, and how this differs from how GlgA binds it acceptor, glycogen. . The structures were superposed on the C-terminal domain and thus emphasize the shift in the N-terminal domain, which is indicated by the two-headed magenta arrow; the magenta asterisk marks the approximate pivot point. . The conserved GlgM (cream carbons) and EcGS (grey carbons; PDB entry 2qzs) donor binding site displaying a superposition of structurally equivalent key residues (labels refer to GlgM only; see main text for E. coli numbering). Also shown are the ADP and α-D-glucose (GLC) ligands (green carbons) bound to EcGS. References
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