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

IUCr IT WDC

home archive editors for authors for readers submit subscribe open access

view article

Figure 4
The similar active-site architecture. (a) Superposition of the −1 subsites of DrTS-N253A–Tris (megenta), XaSH-E322Q–sucrose (slate), NpAS-E328Q–maltoheptaose (green) and RhSI-E254Q–sucrose (yellow). The residue numbering is labelled in the same colour for each protein. The conserved active-site residues of DrTS occupy similar spatial positions to those of XaSH, NpAS and RhSI. Interestingly, the nonreducing terminal maltosyl residue in the NpAS–maltoheptaose complex fits the −1 and +1 subsites of DrTS well. (b)–(d) The interaction networks between the catalytic triad and the surrounding residues in DrTS-N253A–Tris (b), XaSH-E322Q–sucrose (c) and RhSI-E254Q–sucrose (d). The triad residues are indicated by an asterisk.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

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

doi:10.1107/S1399004714022500

Follow Acta Cryst. D

Search term		doi		Advanced search
Author		volume	page