7CJ5
Crystal structure of homo dimeric D-allulose 3-epimerase from Methylomonas sp. in complex with D-fructose
7CJ5 の概要
エントリーDOI | 10.2210/pdb7cj5/pdb |
関連するPDBエントリー | 7CJ4 |
分子名称 | Epimerase, MANGANESE (II) ION, D-fructose, ... (6 entities in total) |
機能のキーワード | epimerase, tim barrel, isomerase |
由来する生物種 | Methylomonas sp. DH-1 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 65313.49 |
構造登録者 | |
主引用文献 | 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 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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