5Z73

Crystal structure of alkaline/neutral invertase InvB from Anabaena sp. PCC 7120

5Z73 の概要

• エントリーDOI: 10.2210/pdb5z73/pdb
• 分子名称: Alr0819 protein, GLYCEROL (3 entities in total)
• 機能のキーワード: alkaline/neutral invertases, cyanobacteria, glycoside hydrolase family 100, sucrose hydrolysis, hydrolase
• 由来する生物種: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 105311.13

構造登録者

Xie, J.,Hu, H.X.,Cai, K.,Yang, F.,Jiang, Y.L.,Chen, Y.,Zhou, C.Z. (登録日: 2018-01-27, 公開日: 2018-05-30, 最終更新日: 2024-11-13)

主引用文献

Xie, J.,Hu, H.X.,Cai, K.,Xia, L.Y.,Yang, F.,Jiang, Y.L.,Chen, Y.,Zhou, C.Z.
Structural and enzymatic analyses of Anabaena heterocyst-specific alkaline invertase InvB.
FEBS Lett., 592:1589-1601, 2018

PubMed Abstract: Anabaena sp. PCC 7120 encodes two alkaline/neutral invertases, namely InvA and InvB. Following our recently reported InvA structure, here we report the crystal structure of the heterocyst-specific InvB. Despite sharing an overall structure similar to InvA, InvB possesses a much higher catalytic activity. Structural comparisons of the catalytic pockets reveal that Arg430 of InvB adopts a different conformation, which may facilitate the deprotonation of the catalytic residue Glu415. We propose that the higher activity may be responsible for the vital role of InvB in heterocyst development and nitrogen fixation. Furthermore, phylogenetic analysis combined with activity assays also suggests the role of this highly conserved arginine in plants and cyanobacteria, as well as some proteobacteria living in highly extreme environments.

PubMed: 29578606
DOI: 10.1002/1873-3468.13041

実験手法

X-RAY DIFFRACTION (1.93 Å)