1E8P

Characterisation of the cellulose docking domain from Piromyces equi

1E8P の概要

• エントリーDOI: 10.2210/pdb1e8p/pdb
• 関連するPDBエントリー: 1E8Q
• NMR情報: BMRB: 3322
• 分子名称: Endoglucanase 45A (1 entity in total)
• 機能のキーワード: cellulose docking domain, cellulase
• 由来する生物種: Piromyces equi
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5044.32

構造登録者

Raghothama, S.,Eberhardt, R.Y.,White, P.,Hazlewood, G.P.,Gilbert, H.J.,Simpson, P.J.,Williamson, M.P. (登録日: 2000-09-28, 公開日: 2001-09-07, 最終更新日: 2024-11-13)

主引用文献

Raghothama, S.,Eberhardt, R.Y.,Simpson, P.,Wigelsworth, D.,White, P.,Hazlewood, G.P.,Nagy, T.,Gilbert, H.J.,Williamson, M.P.
Characterization of a cellulosome dockerin domain from the anaerobic fungus Piromyces equi.
Nat. Struct. Biol., 8:775-778, 2001

PubMed Abstract: The recycling of photosynthetically fixed carbon in plant cell walls is a key microbial process. In anaerobes, the degradation is carried out by a high molecular weight multifunctional complex termed the cellulosome. This consists of a number of independent enzyme components, each of which contains a conserved dockerin domain, which functions to bind the enzyme to a cohesin domain within the protein scaffoldin protein. Here we describe the first three-dimensional structure of a fungal dockerin, the N-terminal dockerin of Cel45A from the anaerobic fungus Piromyces equi. The structure contains a novel fold of 42 residues. The ligand binding site consists of residues Trp 35, Tyr 8 and Asp 23, which are conserved in all fungal dockerins. The binding site is on the opposite side of the N- and C-termini of the molecule, implying that tandem dockerin domains, seen in the majority of anaerobic fungal plant cell wall degrading enzymes, could present multiple simultaneous binding sites and, therefore, permit tailoring of binding to catalytic demands.

PubMed: 11524680
DOI: 10.1038/nsb0901-775

実験手法

SOLUTION NMR