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 2
Ribbon views of the DrTS dimer (a) and monomer (b) structures. The protein consists of a (β/α)₈ barrel (red), subdomain B (blue), domain C (cyan) and two TS-unique modules (S7 in green and S8 in yellow). The bound Mg²⁺ and Ca²⁺ ions are shown as green and magenta spheres, respectively, with the Tris molecule shown as a stick representation. The dimeric interfaces are formed mainly by domain C and S8 and have a total buried area of ∼3000 Å².

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

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

doi:10.1107/S1399004714022500

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