2WCU

Crystal structure of mammalian FucU

2WCU の概要

• エントリーDOI: 10.2210/pdb2wcu/pdb
• 関連するPDBエントリー: 2WCV
• 分子名称: PROTEIN FUCU HOMOLOG, alpha-L-fucopyranose (3 entities in total)
• 機能のキーワード: fucu, fucose, ribose, pyranase, mutarotase, alternative splicing, isomerase
• 由来する生物種: MUS MUSCULUS (MOUSE)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33267.05

構造登録者

Lee, K.-H.,Kim, M.-S.,Suh, H.-Y.,Ku, B.,Song, Y.-L.,Oh, B.-H. (登録日: 2009-03-17, 公開日: 2009-11-10, 最終更新日: 2023-12-13)

主引用文献

Lee, K.-H.,Ryu, K.-S.,Kim, M.-S.,Suh, H.-Y.,Ku, B.,Song, Y.-L.,Ko, S.,Lee, W.,Oh, B.-H.
Crystal Structures and Enzyme Mechanism of a Dual Fucose Mutarotase/Ribose Pyranase
J.Mol.Biol., 391:178-, 2009

PubMed Abstract: Escherichia coli FucU (Fucose Unknown) is a dual fucose mutarotase and ribose pyranase, which shares 44% sequence identity with its human counterpart. Herein, we report the structures of E. coli FucU and mouse FucU bound to L-fucose and delineate the catalytic mechanisms underlying the interconversion between stereoisomers of fucose and ribose. E. coli FucU forms a decameric toroid with each active site formed by two adjacent subunits. While one subunit provides most of the fucose-interacting residues including a catalytic tyrosine residue, the other subunit provides a catalytic His-Asp dyad. This active-site feature is critical not only for the mutarotase activity toward L-fucose but also for the pyranase activity toward D-ribose. Structural and biochemical analyses pointed that mouse FucU assembles into four different oligomeric forms, among which the smallest homodimeric form is most abundant and would be the predominant species under physiological conditions. This homodimer has two fucose-binding sites that are devoid of the His-Asp dyad and catalytically inactive, indicating that the mutarotase and the pyranase activities appear dispensable in vertebrates. The defective assembly of the mouse FucU homodimer into the decameric form is due to an insertion of two residues at the N-terminal extreme, which is a common aspect of all the known vertebrate FucU proteins. Therefore, vertebrate FucU appears to serve for as yet unknown function through the quaternary structural alteration.

PubMed: 19524593
DOI: 10.1016/J.JMB.2009.06.022

実験手法

X-RAY DIFFRACTION (1.9 Å)