7CPK

Xylanase R from Bacillus sp. TAR-1

Summary for 7CPK

• Entry DOI: 10.2210/pdb7cpk/pdb
• Descriptor: Endo-1,4-beta-xylanase A, (4S)-2-METHYL-2,4-PENTANEDIOL, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: gh10, thermostabilation, xylanase, hydrolase
• Biological source: Bacillus sp. TAR1
• Total number of polymer chains: 1
• Total formula weight: 42505.10

Authors

Kuwata, K.,Suzuki, M.,Takita, T.,Nakatani, K.,Li, T.,Katano, Y.,Kojima, K.,Mizutani, K.,Mikami, B.,Yatsunami, R.,Nakamura, S.,Yasukawa, K. (deposition date: 2020-08-07, release date: 2020-09-02, Last modification date: 2023-11-29)

Primary citation

Suzuki, M.,Takita, T.,Kuwata, K.,Nakatani, K.,Li, T.,Katano, Y.,Kojima, K.,Mizutani, K.,Mikami, B.,Yatsunami, R.,Nakamura, S.,Yasukawa, K.
Insight into the mechanism of thermostabilization of GH10 xylanase from Bacillus sp. strain TAR-1 by the mutation of S92 to E.
Biosci.Biotechnol.Biochem., 85:386-390, 2021

PubMed Abstract: The mechanism of thermostabilization of GH10 xylanase, XynR, from Bacillus sp. strain TAR-1 by the mutation of S92 to E was investigated. Thermodynamic analysis revealed that thermostabilization was driven by the decrease in entropy change of activation for thermal inactivation. Crystallographic analysis suggested that this mutation suppressed the fluctuation of the amino acid residues at position 92-95.

PubMed: 33604642
DOI: 10.1093/bbb/zbaa003

Experimental method

X-RAY DIFFRACTION (1.6 Å)