6F04

N-acetylglucosamine-2-epimerase

6F04 の概要

• エントリーDOI: 10.2210/pdb6f04/pdb
• 分子名称: N-acetylglucosamine-2-epimerase, CHLORIDE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: n-acetylglucosamine-2-epimerase, sugar binding protein
• 由来する生物種: Nostoc sp. KVJ10
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47249.78

構造登録者

Halsoer, M.J.,Rothweiler, U. (登録日: 2017-11-17, 公開日: 2018-09-26, 最終更新日: 2024-01-17)

主引用文献

Halsor, M.J.H.,Rothweiler, U.,Altermark, B.,Raeder, I.L.U.
The crystal structure of the N-acetylglucosamine 2-epimerase from Nostoc sp. KVJ10 reveals the true dimer.
Acta Crystallogr D Struct Biol, 75:90-100, 2019

PubMed Abstract: N-Acetylglucosamine 2-epimerases (AGEs) catalyze the interconversion of N-acetylglucosamine and N-acetylmannosamine. They can be used to perform the first step in the synthesis of sialic acid from N-acetylglucosamine, which makes the need for efficient AGEs a priority. This study presents the structure of the AGE from Nostoc sp. KVJ10 collected in northern Norway, referred to as nAGE10. It is the third AGE structure to be published to date, and the first one in space group P422. The nAGE10 monomer folds as an (α/α) barrel in a similar manner to that of the previously published AGEs, but the crystal did not contain the dimers that have previously been reported. The previously proposed `back-to-back' assembly involved the face of the AGE monomer where the barrel helices are connected by small loops. Instead, a `front-to-front' dimer was found in nAGE10 involving the long loops that connect the barrel helices at this end. This assembly is also present in the other AGE structures, but was attributed to crystal packing, even though the `front' interface areas are larger and are more conserved than the `back' interface areas. In addition, the front-to-front association allows a better explanation of the previously reported observations considering surface cysteines. Together, these results indicate that the `front-to-front' dimer is the most probable biological assembly for AGEs.

PubMed: 30644848
DOI: 10.1107/S2059798318017047

実験手法

X-RAY DIFFRACTION (1.699 Å)