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TitleInsight into the mechanism of thermostabilization of GH10 xylanase from Bacillus sp. strain TAR-1 by the mutation of S92 to E.
Journal, issue, pagesBiosci. Biotechnol. Biochem., Vol. 85, Page 386-390, Year 2021
Publish dateAug 7, 2020 (structure data deposition date)
AuthorsSuzuki, M. / Takita, T. / Kuwata, K. / Nakatani, K. / Li, T. / Katano, Y. / Kojima, K. / Mizutani, K. / Mikami, B. / Yatsunami, R. ...Suzuki, M. / Takita, T. / Kuwata, K. / Nakatani, K. / Li, T. / Katano, Y. / Kojima, K. / Mizutani, K. / Mikami, B. / Yatsunami, R. / Nakamura, S. / Yasukawa, K.
External linksBiosci. Biotechnol. Biochem. / PubMed:33604642
MethodsX-ray diffraction
Resolution1.52 - 1.6 Å
Structure data

PDB-7cpk:
Xylanase R from Bacillus sp. TAR-1
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-7cpl:
Xylanase R from Bacillus sp. TAR-1
Method: X-RAY DIFFRACTION / Resolution: 1.52 Å

Chemicals

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

ChemComp-CA:
Unknown entry

ChemComp-NI:
NICKEL (II) ION

ChemComp-HOH:
WATER

Source
  • bacillus sp. tar1 (bacteria)
KeywordsHYDROLASE / GH10 / thermostabilation / xylanase

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