5Y3X

Crystal structure of endo-1,4-beta-xylanase from Caldicellulosiruptor owensensis

Summary for 5Y3X

• Entry DOI: 10.2210/pdb5y3x/pdb
• Descriptor: Beta-xylanase (2 entities in total)
• Functional Keywords: gh10 xylanase, thermostability, hydrolase
• Biological source: Caldicellulosiruptor owensensis OL
• Total number of polymer chains: 6
• Total formula weight: 254562.80

Authors

Liu, X.,Sun, L.C.,Zhang, Y.B.,Liu, T.F.,Xin, F.J. (deposition date: 2017-07-31, release date: 2017-12-27, Last modification date: 2023-11-22)

Primary citation

Liu, X.,Liu, T.,Zhang, Y.,Xin, F.,Mi, S.,Wen, B.,Gu, T.,Shi, X.,Wang, F.,Sun, L.
Structural Insights into the Thermophilic Adaption Mechanism of Endo-1,4-beta-Xylanase from Caldicellulosiruptor owensensis.
J. Agric. Food Chem., 66:187-193, 2018

PubMed Abstract: Xylanases (EC 3.2.1.8) are a kind of enzymes degrading xylan to xylooligosaccharides (XOS) and have been widely used in a variety of industrial applications. Among them, xylanases from thermophilic microorganisms have distinct advantages in industries that require high temperature conditions. The CoXynA gene, encoding a glycoside hydrolase (GH) family 10 xylanase, was identified from thermophilic Caldicellulosiruptor owensensis and was overexpressed in Escherichia coli. Recombinant CoXynA showed optimal activity at 90 °C with a half-life of about 1 h at 80 °C and exhibited highest activity at pH 7.0. The activity of CoXynA activity was affected by a variety of cations. CoXynA showed distinct substrate specificities for beechwood xylan and birchwood xylan. The crystal structure of CoXynA was solved and a molecular dynamics simulation of CoXynA was performed. The relatively high thermostability of CoXynA was proposed to be due to the increased overall protein rigidity resulting from the reduced length and fluctuation of Loop 7.

PubMed: 29236500
DOI: 10.1021/acs.jafc.7b03607

Experimental method

X-RAY DIFFRACTION (2.1 Å)