5Z73

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

Summary for 5Z73

• Entry DOI: 10.2210/pdb5z73/pdb
• Descriptor: Alr0819 protein, GLYCEROL (3 entities in total)
• Functional Keywords: alkaline/neutral invertases, cyanobacteria, glycoside hydrolase family 100, sucrose hydrolysis, hydrolase
• Biological source: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
• Total number of polymer chains: 2
• Total formula weight: 105311.13

Authors

Xie, J.,Hu, H.X.,Cai, K.,Yang, F.,Jiang, Y.L.,Chen, Y.,Zhou, C.Z. (deposition date: 2018-01-27, release date: 2018-05-30, Last modification date: 2024-11-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.93 Å)