3WDV

The complex structure of PtLic16A with cellotetraose

Summary for 3WDV

• Entry DOI: 10.2210/pdb3wdv/pdb
• Related: 3WDT 3WDU 3WDW 3WDX 3WDY
• Related PRD ID: PRD_900005
• Descriptor: Beta-1,3-1,4-glucanase, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: 1, 3-1, 4-beta-glucanase, 3(4)-beta-glucanase, ptlic16a, beta-jellyroll fold, hydrolase
• Biological source: Paecilomyces (Paecilomyces thermophila)
• Total number of polymer chains: 4
• Total formula weight: 130722.29

Authors

Cheng, Y.S.,Huang, C.H.,Chen, C.C.,Huang, T.Y.,Ko, T.P.,Huang, J.W.,Wu, T.H.,Liu, J.R.,Guo, R.T. (deposition date: 2013-06-25, release date: 2014-07-09, Last modification date: 2024-10-30)

Primary citation

Cheng, Y.S.,Huang, C.H.,Chen, C.C.,Huang, T.Y.,Ko, T.P.,Huang, J.W.,Wu, T.H.,Liu, J.R.,Guo, R.T.
Structural and mutagenetic analyses of a 1,3-1,4-beta-glucanase from Paecilomyces thermophila
Biochim.Biophys.Acta, 1844:366-373, 2014

PubMed Abstract: The thermostable 1,3-1,4-β-glucanase PtLic16A from the fungus Paecilomyces thermophila catalyzes stringent hydrolysis of barley β-glucan and lichenan with an outstanding efficiency and has great potential for broad industrial applications. Here, we report the crystal structures of PtLic16A and an inactive mutant E113A in ligand-free form and in complex with the ligands cellobiose, cellotetraose and glucotriose at 1.80Å to 2.25Å resolution. PtLic16A adopts a typical β-jellyroll fold with a curved surface and the concave face forms an extended ligand binding cleft. These structures suggest that PtLic16A might carry out the hydrolysis via retaining mechanism with E113 and E118 serving as the nucleophile and general acid/base, respectively. Interestingly, in the structure of E113A/1,3-1,4-β-glucotriose complex, the sugar bound to the -1 subsite adopts an intermediate-like (α-anomeric) configuration. By combining all crystal structures solved here, a comprehensive binding mode for a substrate is proposed. These findings not only help understand the 1,3-1,4-β-glucanase catalytic mechanism but also provide a basis for further enzymatic engineering.

PubMed: 24262091
DOI: 10.1016/j.bbapap.2013.11.005

Experimental method

X-RAY DIFFRACTION (1.936 Å)