5NS7

Crystal structure of beta-glucosidase BglM-G1 mutant H75R from marine metagenome

5NS7 の概要

• エントリーDOI: 10.2210/pdb5ns7/pdb
• 分子名称: beta-glucosidase M - G1, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: hydrolase, beta-glucosidase, metagenomes
• 由来する生物種: marine metagenome
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 157866.46

構造登録者

Mhaindarkar, D.C.,Gasper, R.,Lupilova, N.,Leichert, L.I.,Hofmann, E. (登録日: 2017-04-25, 公開日: 2018-08-08, 最終更新日: 2024-05-08)

主引用文献

Mhaindarkar, D.,Gasper, R.,Lupilov, N.,Hofmann, E.,Leichert, L.I.
Loss of a conserved salt bridge in bacterial glycosyl hydrolase BgIM-G1 improves substrate binding in temperate environments.
Commun Biol, 1:171-171, 2018

PubMed Abstract: Salt bridges are the strongest electrostatic interactions in proteins. They substantially contribute to a protein's structural stability. Thus, mutations of salt bridges are typically selected against. Here, we report on the evolutionary loss of a highly conserved salt bridge in the GH1 family glycosyl hydrolase BglM-G1. BglM-G1's gene was found in the bacterial metagenome of a temperate, seasonally cold marine habitat. In BglM-G1, arginine 75 is replaced by a histidine. While fully retaining β-glucosidase activity, BglM-G1 is less heat stable than an H75R variant, in which the salt bridge was artificially re-introduced. However, the toward its substrates was lower in wild type, leading to an overall higher catalytic efficiency. Our results indicate that this loss of the salt bridge leads to higher flexibility in BglM-G1's active site, trading structural stability at high temperatures, a trait not needed in a temperate, seasonally cold habitat, for a more effective catalytic activity.

PubMed: 30345395
DOI: 10.1038/s42003-018-0167-7

実験手法

X-RAY DIFFRACTION (1.54 Å)