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

Yung Lin Wang (Contributor)
Sih Yao Chow (Contributor)
Yi Ting Lin (Contributor)
Yu Chiao Hsieh (Contributor)
Guan-Chiun Lee (Contributor)
Shwu Huey Liaw (Contributor)
Jia Hung Wang (Contributor)
Meng Yin Tsai (Contributor)
Jen Jye Chen (Contributor)
Jei Fu Shaw (Contributor)

Dataset

Date made available	2014 Dec 24
Publisher	Protein Data Bank (PDB)

DOI
10.2210/pdb4WF7/pdb

Access Dataset

https://www.wwpdb.org/pdb?id=pdb_00004wf7

1 Article

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., 2014 Dec 1, In: Acta Crystallographica Section D: Biological Crystallography. 70, 12, p. 3144-3154 11 p.
Research output: Contribution to journal › Article › peer-review

Open Access
20 Citations (Scopus)

Cite this

Wang, Y. (Contributor), Chow, S. (Contributor), Lin, Y. (Contributor), Hsieh, Y. (Contributor), Lee, G. (Contributor), Liaw, S. (Contributor), Wang, J. (Contributor), Tsai, M. (Contributor), Chen, J. (Contributor), Shaw, J. (Contributor) (2014 Dec 24). Crystal structures of trehalose synthase from Deinococcus radiodurans reveal that a closed conformation is involved in the intramolecular isomerization catalysis. Protein Data Bank (PDB). 10.2210/pdb4WF7/pdb

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

DOI

Access Dataset

Research output

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

Cite this