1E8Q

Characterisation of the cellulose docking domain from Piromyces equi

Summary for 1E8Q

• Entry DOI: 10.2210/pdb1e8q/pdb
• Related: 1E8P
• NMR Information: BMRB: 3322
• Descriptor: Endoglucanase 45A (1 entity in total)
• Functional Keywords: cellulose docking domain, cellulase
• Biological source: Piromyces equi
• Total number of polymer chains: 1
• Total formula weight: 5044.32

Authors

Raghothama, S.,Eberhardt, R.Y.,White, P.,Hazlewood, G.P.,Gilbert, H.J.,Simpson, P.J.,Williamson, M.P. (deposition date: 2000-09-28, release date: 2001-09-07, Last modification date: 2024-11-13)

Primary citation

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

Experimental method

SOLUTION NMR