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5GOQ

Crystal structure of alkaline invertase InvA from Anabaena sp. PCC 7120 complexed with glucose

Summary for 5GOQ
Entry DOI10.2210/pdb5goq/pdb
Related5GOO 5GOP 5GOR
DescriptorAlkaline Invertase, alpha-D-glucopyranose (3 entities in total)
Functional Keywordsalkaline invertases, cyanobacteria, glycoside hydrolase family 100, sucrose hydrolysis, hydrolase
Biological sourceNostoc sp. PCC 7120
Total number of polymer chains3
Total formula weight160518.00
Authors
Xie, J.,Cai, K.,Hu, H.X.,Jiang, Y.L.,Yang, F.,Hu, P.F.,Chen, Y.,Zhou, C.Z. (deposition date: 2016-07-28, release date: 2016-11-02, Last modification date: 2024-10-16)
Primary citationXie, J.,Cai, K.,Hu, H.X.,Jiang, Y.L.,Yang, F.,Hu, P.F.,Cao, D.D.,Li, W.F.,Chen, Y.,Zhou, C.Z.
Structural Analysis of the Catalytic Mechanism and Substrate Specificity of Anabaena Alkaline Invertase InvA Reveals a Novel Glucosidase
J. Biol. Chem., 291:25667-25677, 2016
Cited by
PubMed Abstract: Invertases catalyze the hydrolysis of sucrose to glucose and fructose, thereby playing a key role in primary metabolism and plant development. According to the optimum pH, invertases are classified into acid invertases (Ac-Invs) and alkaline/neutral invertases (A/N-Invs), which share no sequence homology. Compared with Ac-Invs that have been extensively studied, the structure and catalytic mechanism of A/N-Invs remain unknown. Here we report the crystal structures of Anabaena alkaline invertase InvA, which was proposed to be the ancestor of modern plant A/N-Invs. These structures are the first in the GH100 family. InvA exists as a hexamer in both crystal and solution. Each subunit consists of an (α/α) barrel core structure in addition to an insertion of three helices. A couple of structures in complex with the substrate or products enabled us to assign the subsites -1 and +1 specifically binding glucose and fructose, respectively. Structural comparison combined with enzymatic assays indicated that Asp-188 and Glu-414 are putative catalytic residues. Further analysis of the substrate binding pocket demonstrated that InvA possesses a stringent substrate specificity toward the α1,2-glycosidic bond of sucrose. Together, we suggest that InvA and homologs represent a novel family of glucosidases.
PubMed: 27777307
DOI: 10.1074/jbc.M116.759290
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.75 Å)
Structure validation

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