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5ZFS

Crystal structure of Arthrobacter globiformis M30 sugar epimerase which can produce D-allulose from D-fructose

Summary for 5ZFS
Entry DOI10.2210/pdb5zfs/pdb
DescriptorD-allulose-3-epimerase, MANGANESE (II) ION, ACETATE ION, ... (4 entities in total)
Functional Keywordsepimerase, isomerase
Biological sourceArthrobacter globiformis
Total number of polymer chains2
Total formula weight65429.98
Authors
Yoshida, H.,Yoshihara, A.,Gullapalli, P.K.,Ohtani, K.,Akimitsu, K.,Izumori, K.,Kamitori, S. (deposition date: 2018-03-07, release date: 2018-10-24, Last modification date: 2023-11-22)
Primary citationYoshida, H.,Yoshihara, A.,Gullapalli, P.K.,Ohtani, K.,Akimitsu, K.,Izumori, K.,Kamitori, S.
X-ray structure of Arthrobacter globiformis M30 ketose 3-epimerase for the production of D-allulose from D-fructose.
Acta Crystallogr F Struct Biol Commun, 74:669-676, 2018
Cited by
PubMed Abstract: The X-ray structure of ketose 3-epimerase from Arthrobacter globiformis M30, which was previously reported to be a D-allulose 3-epimerase (AgD-AE), was determined at 1.96 Å resolution. The crystal belonged to the hexagonal space group P622, with unit-cell parameters a = b = 103.98, c = 256.53 Å. The structure was solved by molecular replacement using the structure of Mesorhizobium loti L-ribulose 3-epimerase (MlL-RE), which has 41% sequence identity, as a search model. A hexagonal crystal contained two molecules in the asymmetric unit, and AgD-AE formed a homotetramer with twofold symmetry. The overall structure of AgD-AE was more similar to that of MlL-RE than to the known structures of D-psicose (alternative name D-allulose) 3-epimerases (D-PEs or D-AEs), although AgD-AE and MlL-RE have different substrate specificities. Both AgD-AE and MlL-RE have long helices in the C-terminal region that would contribute to the stability of the homotetramer. AgD-AE showed higher enzymatic activity for L-ribulose than D-allulose; however, AgD-AE is stable and is a unique useful enzyme for the production of D-allulose from D-fructose.
PubMed: 30279320
DOI: 10.1107/S2053230X18011706
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.96 Å)
Structure validation

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건을2025-08-06부터공개중

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