3WUE
The wild type crystal structure of b-1,4-Xylanase (XynAS9) with xylobiose from Streptomyces sp. 9
Summary for 3WUE
| Entry DOI | 10.2210/pdb3wue/pdb |
| Related | 3WUB 3WUF 3WUG |
| Related PRD ID | PRD_900116 |
| Descriptor | Endo-1,4-beta-xylanase A, beta-D-xylopyranose-(1-4)-beta-D-xylopyranose, ZINC ION, ... (4 entities in total) |
| Functional Keywords | beta-1, 4-xylanase, thermozyme, protein engineering, protein rigidity, hydrolase |
| Biological source | Streptomyces sp. |
| Total number of polymer chains | 1 |
| Total formula weight | 35502.98 |
| Authors | Chen, C.C.,Han, X.,Lv, P.,Ko, T.P.,Peng, W.,Huang, C.H.,Zheng, Y.,Gao, J.,Yang, Y.,Guo, R.T. (deposition date: 2014-04-23, release date: 2014-10-29, Last modification date: 2023-11-08) |
| Primary citation | Chen, C.C.,Luo, H.,Han, X.,Lv, P.,Ko, T.P.,Peng, W.,Huang, C.H.,Wang, K.,Gao, J.,Zheng, Y.,Yang, Y.,Zhang, J.,Yao, B.,Guo, R.T. Structural perspectives of an engineered beta-1,4-xylanase with enhanced thermostability. J.Biotechnol., 189C:175-182, 2014 Cited by PubMed Abstract: The glycoside hydrolase 10 (GH10) xylanase from Streptomyces sp. 9 (XynAS9) can operate in a broad range of pH and temperature, and thus is a potential candidate for commercial applications. Recently, we engineered XynAS9 via mutating several residues in accordance with the consensus sequences of GH10 thermophilic xylanases in an attempt to improve the enzyme thermostability and thermotolerance. The most promising effects were observed in the double mutant V81P/G82E. In order to investigate the molecular mechanism of the improved thermal profile of XynAS9, complex crystal structures of the wild type (WT) and mutant (MT) enzyme were solved at 1.88-2.05Å resolution. The structures reveal a classical GH10 (β/α)8 TIM-barrel fold. In MT XynAS9, E82 forms several interactions to its neighboring residues, which might aid in stabilizing the local structure. Furthermore, the MT structure showed lower B factors for individual residues compared to the WT structure, reflecting the increased MT protein rigidity. Analyses of the XynAS9 structures also delineate the detailed enzyme-substrate interaction network. More importantly, possible explanations for the enhanced thermal profiles of MT XynAS9 are proposed, which may be a useful strategy for enzyme engineering in the future. PubMed: 25193708DOI: 10.1016/j.jbiotec.2014.08.030 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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