5D8Z

Structrue of a lucidum protein

Summary for 5D8Z

• Entry DOI: 10.2210/pdb5d8z/pdb
• Related: 5D8W
• Related PRD ID: PRD_900005
• Descriptor: endoglucanase, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: gh5 family, ganoderma lucidum, endoglucanase, hydrolase
• Biological source: Ganoderma lucidum
• Total number of polymer chains: 2
• Total formula weight: 74160.59

Authors

Guo, R.,Li, Q.,Shang, N.,Liu, G.,Ko, T.P.,Chen, C.C.,Liu, W. (deposition date: 2015-08-18, release date: 2016-06-29, Last modification date: 2024-10-09)

Primary citation

Liu, G.,Li, Q.,Shang, N.,Huang, J.W.,Ko, T.P.,Liu, W.,Zheng, Y.,Han, X.,Chen, Y.,Chen, C.C.,Jin, J.,Guo, R.T.
Functional and structural analyses of a 1,4-beta-endoglucanase from Ganoderma lucidum.
Enzyme.Microb.Technol., 86:67-74, 2016

PubMed Abstract: Ganoderma lucidum is a saprotrophic white-rot fungus which contains a rich set of cellulolytic enzymes. Here, we screened an array of potential 1,4-β-endoglucanases from G. lucidum based on the gene annotation library and found that one candidate gene, GlCel5A, exhibits CMC-hydrolyzing activity. The recombinant GlCel5A protein expressed in Pichia pastoris is able to hydrolyze CMC and β-glucan but not xylan and mannan. The enzyme exhibits optimal activity at 60°C and pH 3-4, and retained 50% activity at 80 and 90°C for at least 15 and 10min. The crystal structure of GlCel5A and its complex with cellobiose, solved at 2.7 and 2.86Å resolution, shows a classical (β/α)8 TIM-barrel fold as seen in other members of glycoside hydrolase family 5. The complex structure contains a cellobiose molecule in the +1 and +2 subsites, and reveals the interactions with the positive sites of the enzyme. Collectively, the present work provides the first comprehensive characterization of an endoglucanase from G. lucidum that possesses properties for industrial applications, and strongly encourages further studying in the cellulolytic enzyme system of G. lucidum.

PubMed: 26992795
DOI: 10.1016/j.enzmictec.2016.01.013

Experimental method

X-RAY DIFFRACTION (2.7 Å)