5I0E

Cycloalternan-degrading enzyme from Trueperella pyogenes in complex with isomaltose

5I0E の概要

• エントリーDOI: 10.2210/pdb5i0e/pdb
• 関連するPDBエントリー: 5I0D 5I0F 5I0G
• 分子名称: Glycoside hydrolase family 31, alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, structural genomics, center for structural genomics of infectious diseases, csgid, sugar binding protein
• 由来する生物種: Trueperella pyogenes
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 82986.17

構造登録者

Light, S.H.,Minasov, G.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (登録日: 2016-02-03, 公開日: 2016-12-14, 最終更新日: 2023-09-27)

主引用文献

Light, S.H.,Cahoon, L.A.,Mahasenan, K.V.,Lee, M.,Boggess, B.,Halavaty, A.S.,Mobashery, S.,Freitag, N.E.,Anderson, W.F.
Transferase Versus Hydrolase: The Role of Conformational Flexibility in Reaction Specificity.
Structure, 25:295-304, 2017

PubMed Abstract: Active in the aqueous cellular environment where a massive excess of water is perpetually present, enzymes that catalyze the transfer of an electrophile to a non-water nucleophile (transferases) require specific strategies to inhibit mechanistically related hydrolysis reactions. To identify principles that confer transferase versus hydrolase reaction specificity, we exploited two enzymes that use highly similar catalytic apparatuses to catalyze the transglycosylation (a transferase reaction) or hydrolysis of α-1,3-glucan linkages in the cyclic tetrasaccharide cycloalternan (CA). We show that substrate binding to non-catalytic domains and a conformationally stable active site promote CA transglycosylation, whereas a distinct pattern of active site conformational change is associated with CA hydrolysis. These findings defy the classic view of induced-fit conformational change and illustrate a mechanism by which a stable hydrophobic binding site can favor transferase activity and disfavor hydrolysis. Application of these principles could facilitate the rational reengineering of transferases with desired catalytic properties.

PubMed: 28089449
DOI: 10.1016/j.str.2016.12.007

実験手法

X-RAY DIFFRACTION (2.3 Å)