5BV9

The Structure of Bacillus pumilus GH48 in complex with cellobiose

5BV9 の概要

• エントリーDOI: 10.2210/pdb5bv9/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900005
• 分子名称: Cellulose 1,4-beta-cellobiosidase, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, CALCIUM ION, ... (8 entities in total)
• 機能のキーワード: gh48, cellulase, cellobiose, hydrolase
• 由来する生物種: Bacillus pumilus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 81417.99

構造登録者

Alahuhta, P.M.,Lunin, V.V. (登録日: 2015-06-04, 公開日: 2015-09-30, 最終更新日: 2023-09-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.93 Å)