Crystal structure of trehalose synthase from Deinococcus radiodurans reveals a closed conformation for catalysis of the intramolecular isomerization

Yung Lin Wang (Contributor)
Sih Yao Chow (Contributor)
Yi Ting Lin (Contributor)
Yu Chiao Hsieh (Contributor)
Guan-Chiun Lee (Ming Chuan University) (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 17
Publisher	Protein Data Bank (PDB)

DOI
10.2210/pdb4TVU/pdb

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https://www.wwpdb.org/pdb?id=pdb_00004tvu

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
22 Link opens in a new tab Citations (Scopus)

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DataSetCite

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 17). Crystal structure of trehalose synthase from Deinococcus radiodurans reveals a closed conformation for catalysis of the intramolecular isomerization. Protein Data Bank (PDB). 10.2210/pdb4TVU/pdb

Crystal structure of trehalose synthase from Deinococcus radiodurans reveals a closed conformation for catalysis of the intramolecular isomerization

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