5AYC

Crystal structure of Ruminococcus albus 4-O-beta-D-mannosyl-D-glucose phosphorylase (RaMP1) in complexes with sulfate and 4-O-beta-D-mannosyl-D-glucose

5AYC の概要

• エントリーDOI: 10.2210/pdb5ayc/pdb
• 関連するPDBエントリー: 5AY9 5AYD 5AYE
• 分子名称: 4-O-beta-D-mannosyl-D-glucose phosphorylase, beta-D-mannopyranose-(1-4)-beta-D-glucopyranose, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: glycoside hydrolase family 130, transferase
• 由来する生物種: Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44138.36

構造登録者

Ye, Y.,Saburi, W.,Kato, K.,Yao, M. (登録日: 2015-08-13, 公開日: 2016-03-23, 最終更新日: 2024-03-20)

主引用文献

Ye, Y.,Saburi, W.,Odaka, R.,Kato, K.,Sakurai, N.,Komoda, K.,Nishimoto, M.,Kitaoka, M.,Mori, H.,Yao, M.
Structural insights into the difference in substrate recognition of two mannoside phosphorylases from two GH130 subfamilies.
Febs Lett., 590:828-837, 2016

PubMed Abstract: In Ruminococcus albus, 4-O-β-D-mannosyl-D-glucose phosphorylase (RaMP1) and β-(1,4)-mannooligosaccharide phosphorylase (RaMP2) belong to two subfamilies of glycoside hydrolase family 130. The two enzymes phosphorolyze β-mannosidic linkages at the nonreducing ends of their substrates, and have substantially diverse substrate specificity. The differences in their mechanism of substrate binding have not yet been fully clarified. In the present study, we report the crystal structures of RaMP1 with/without 4-O-β-D-mannosyl-d-glucose and RaMP2 with/without β-(1→4)-mannobiose. The structures of the two enzymes differ at the +1 subsite of the substrate-binding pocket. Three loops are proposed to determine the different substrate specificities. One of these loops is contributed from the adjacent molecule of the oligomer structure. In RaMP1, His245 of loop 3 forms a hydrogen-bond network with the substrate through a water molecule, and is indispensible for substrate binding.

PubMed: 26913570
DOI: 10.1002/1873-3468.12105

実験手法

X-RAY DIFFRACTION (1.9 Å)