7CJ8
Crystal structure of N-terminal His-tagged D-allulose 3-epimerase from Methylomonas sp. in complex with D-allulose
Summary for 7CJ8
Entry DOI | 10.2210/pdb7cj8/pdb |
Related | 7CJ4 |
Descriptor | Epimerase, MANGANESE (II) ION, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (5 entities in total) |
Functional Keywords | epimerase, tim barrel, isomerase |
Biological source | Methylomonas sp. DH-1 |
Total number of polymer chains | 6 |
Total formula weight | 204396.54 |
Authors | Yoshida, H.,Yoshihara, A.,Kamitori, S. (deposition date: 2020-07-09, release date: 2021-04-21, Last modification date: 2023-11-29) |
Primary citation | Yoshida, H.,Yoshihara, A.,Kato, S.,Mochizuki, S.,Akimitsu, K.,Izumori, K.,Kamitori, S. Crystal structure of a novel homodimeric l-ribulose 3-epimerase from Methylomonus sp. Febs Open Bio, 11:1621-1637, 2021 Cited by PubMed Abstract: d-Allulose has potential as a low-calorie sweetener which can suppress fat accumulation. Several enzymes capable of d-allulose production have been isolated, including d-tagatose 3-epimerases. Here, we report the isolation of a novel protein from Methylomonas sp. expected to be a putative enzyme based on sequence similarity to ketose 3-epimerase. The synthesized gene encoding the deduced ketose 3-epimerase was expressed as a recombinant enzyme in Escherichia coli, and it exhibited the highest enzymatic activity toward l-ribulose, followed by d-ribulose and d-allulose. The X-ray structure analysis of l-ribulose 3-epimerase from Methylomonas sp. (MetLRE) revealed a homodimeric enzyme, the first reported structure of dimeric l-ribulose 3-epimerase. The monomeric structure of MetLRE is similar to that of homotetrameric l-ribulose 3-epimerases, but the short C-terminal α-helix of MetLRE is unique and different from those of known l-ribulose 3 epimerases. The length of the C-terminal α-helix was thought to be involved in tetramerization and increasing stability; however, the addition of residues to MetLRE at the C terminus did not lead to tetramer formation. MetLRE is the first dimeric l-ribulose 3-epimerase identified to exhibit high relative activity toward d-allulose. PubMed: 33838083DOI: 10.1002/2211-5463.13159 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
Download full validation report