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

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 6
The substrate-binding site in DrTS. (a) The Tris bound at the −1 subsite in the N253A mutant. The simulated-annealing F_o − F_c OMIT map for Tris is contoured at the 6σ level. (b) An additional Tris-binding site in the N253A variant. The simulated-annealing F_o − F_c OMIT map is contoured at the 4σ level. (c) The interaction networks between DrTS and the modelled maltose in the +1 subsite. Hydrogen bonds are shown as green dashed lines. (d) Molecular surfaces of the +1 subsite. The view is the same as that in (c).

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

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

doi:10.1107/S1399004714022500

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