Structures of trehalose synthase from Deinococcus radiodurans reveal that a closed conformation is involved in catalysis of the intramolecular isomerization

Wang, Y.-L.; Chow, S.-Y.; Lin, Y.-T.; Hsieh, Y.-C.; Lee, G.-C.; Liaw, S.-H.

doi:10.1107/S1399004714022500

Figure 3
Closest structural neighbours of DrTS. Structural superpositions of DrTS-N253A–Tris (red), XaSH-E322Q–sucrose (blue; PDB entry 3czk ), NpAS-E328Q–maltoheptaose (green; PDB entry 1mw0 ) and RhSI-E254Q–sucrose (yellow; PDB entry 2pwe ) for the (β/α)₈ barrel (a), subdomain B (b) and domain C (c). These enzymes share a conserved (β/α)₈ barrel, parts of subdomain B and a structurally conserved five-stranded sheet in domain C, particularly the Cβ2, Cβ3 and Cβ7 strands. (d) Structure-based sequence alignment of DrTS and its close homologues. Secondary-structure elements of DrTS are labelled and the numbers of residues in gaps are indicated in parentheses. BtSusG contains an additional carbohydrate-binding module inserted between Bβ2 and Bβ3. The residues of the Mg²⁺ and Ca²⁺ sites are shaded in magenta and cyan, respectively. The substrate-binding residues are shaded in red, whereas the residues of the conserved hydrophobic core are shaded in yellow. The catalytic triad residues are indicated with an asterisk, while the residues involved in stabilization of the triad orientation, but not in substrate binding, are shaded in blue and indicated with a hash, whereas those involved in both functions are shaded in red and indicated with a hash.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 70| Part 12| November 2014| Pages 3144-3154

doi:10.1107/S1399004714022500

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