Davis L. Martinec/Sandbox 4eqv

General Description

4EQV is 469 kDa invertase(SInv) isolated from Saccharomyces cerevisiae. SInv catalyzes the hydrolysis of sucrose into fructose and glucose, thus making it an essential enzyme to plants and other organisms, such as honey bees^[1]. Invertase also lends itself to industry and is extensively used fermentation, where yeast are employed to process sugar into ethanol.

Yeast invertase was first isolated in 1860 by Berthelot, but had been alluded to by Dubrunfaut in 1847.^[2] Invertase was posited to be an intracellular enzymee, yet de la Fuente and Sols were able to show that invertase can be excreted by the cell, thus it is also extracellular^[3]. The intracellular form of the enzyme is not glycosylated, while the extracellular form is extensively glycosylated^[1].

Structure

Catalytic β-propeller Domain

The of 4EQV

The of the β-propeller Domain

β-sandwich Domain

the of invertase

A formed by chain A and chain B showing how each active site is capped by the β-sandwich Domain.

β-sandwich domains form between residues 343-363.

Open & Closed Assembly

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the of chain E

Evolutionary Conservation & Related Proteins

Available Structures

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

References

1. ↑ ^{1.0 1.1} Sainz-Polo MA, Ramirez-Escudero M, Lafraya A, Gonzalez B, Marin-Navarro J, Polaina J, Sanz-Aparicio J. The three-dimensional structure of Saccharomyces invertase: role of a non-catalytic domain in oligomerization and substrate specificity. J Biol Chem. 2013 Feb 21. PMID:23430743 doi:http://dx.doi.org/10.1074/jbc.M112.446435
2. ↑ Sainz-Polo MA, Ramirez-Escudero M, Lafraya A, Gonzalez B, Marin-Navarro J, Polaina J, Sanz-Aparicio J. The three-dimensional structure of Saccharomyces invertase: role of a non-catalytic domain in oligomerization and substrate specificity. J Biol Chem. 2013 Feb 21. PMID:23430743 doi:http://dx.doi.org/10.1074/jbc.M112.446435
3. ↑ https://doi.org/10.1016/0006-3002(62)90526-7