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 8
The interaction networks between subdomains B (magenta) and S7 (blue) in MtTS (PDB entry 4lxf ; chain B) (a), MsTS (b), DrTS–Tris (c) and DrTS-N253A–Tris (d). In one MtTS structure the active site is wide open owing to a disordered region in S7, while in MsTS Leu344 blocks the substrate-binding pocket. On the other hand, in DrTS a closed conformation was observed. These TS structures indicate that subdomains B and S7 serve as a gateway for the opening and closing of the active site. In N253A, the absence of the hydrogen bond between Asn253 and Glu324 causes movement of the Glu324 side chain, leading to the creation of a small pore for water entry.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

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

doi:10.1107/S1399004714022500

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