5BV9

The Structure of Bacillus pumilus GH48 in complex with cellobiose

Summary for 5BV9

• Entry DOI: 10.2210/pdb5bv9/pdb
• Related PRD ID: PRD_900005
• Descriptor: Cellulose 1,4-beta-cellobiosidase, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, CALCIUM ION, ... (8 entities in total)
• Functional Keywords: gh48, cellulase, cellobiose, hydrolase
• Biological source: Bacillus pumilus
• Total number of polymer chains: 1
• Total formula weight: 81417.99

Authors

Alahuhta, P.M.,Lunin, V.V. (deposition date: 2015-06-04, release date: 2015-09-30, Last modification date: 2023-09-27)

Primary citation

Chen, M.,Bu, L.,Alahuhta, M.,Brunecky, R.,Xu, Q.,Lunin, V.V.,Brady, J.W.,Crowley, M.F.,Himmel, M.E.,Bomble, Y.J.
Strategies to reduce end-product inhibition in family 48 glycoside hydrolases.
Proteins, 84:295-304, 2016

PubMed Abstract: Family 48 cellobiohydrolases are some of the most abundant glycoside hydrolases in nature. They are able to degrade cellulosic biomass and therefore serve as good enzyme candidates for biofuel production. Family 48 cellulases hydrolyze cellulose chains via a processive mechanism, and produce end products composed primarily of cellobiose as well as other cellooligomers (dp ≤ 4). The challenge of utilizing cellulases in biofuel production lies in their extremely slow turnover rate. A factor contributing to the low enzyme activity is suggested to be product binding to enzyme and the resulting performance inhibition. In this study, we quantitatively evaluated the product inhibitory effect of four family 48 glycoside hydrolases using molecular dynamics simulations and product expulsion free-energy calculations. We also suggested a series of single mutants of the four family 48 glycoside hydrolases with theoretically reduced level of product inhibition. The theoretical calculations provide a guide for future experimental studies designed to produce mutant cellulases with enhanced activity.

PubMed: 26572060
DOI: 10.1002/prot.24965

Experimental method

X-RAY DIFFRACTION (1.93 Å)