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Characterization of a cellulosome dockerin domain from the anaerobic fungus Piromyces equi

Lookup NU author(s): Tibor Nagy, Emeritus Professor Harry Gilbert

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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.

Publication metadata

Author(s): Raghothama S, Eberhardt RY, Simpson P, Wigelsworth D, White P, Hazlewood GP, Nagy T, Gilbert HJ, Williamson MP

Publication type: Article

Publication status: Published

Journal: Nature Structural Biology

Year: 2001

Volume: 8

Issue: 9

Pages: 775-778

Print publication date: 01/01/2001

ISSN (print): 1072-8368

ISSN (electronic): 1545-9985

Publisher: Nature Publishing Group

URL: http://dx.doi.org/10.1038/nsb0901-775

DOI: 10.1038/nsb0901-775

PubMed id: 11524680

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