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

Nature Structural Biology volume 8, pages 775–778 (2001)Cite this article

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.

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Figure 1: Comparison of the primary sequences of dockerin domains from P. equi polysaccharide hydrolases.
Figure 2: Solution structure of the P. equi dockerin.
Figure 3: 15N T2 values for backbone nitrogens.
Figure 4: Selected binding titration curves for dockerins.

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Acknowledgements

We thank the Biotechnology and Biological Sciences Research Council (BBSRC) for project grants and CASE studentships, Finnfeeds International for financial support, and BBSRC and the Wellcome Trust for equipment grants. The Krebs Institute is a BBSRC Centre. M.P.W., S.R. and P.J.S .are members of the BBSRC-funded North of England Structural Biology Centre.

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Author notes

  1. Harry J. Gilbert

    Present address: Department of Biological and Nutritional Sciences, University of Newcastle upon Tyne, Newcastle upon Tyne, NE1 7RU, UK

  2. S. Raghothama

    Present address: Sophisticated Instruments Facility, Indian Institute of Science, Bangalore, 560 012, India

  3. Ruth Y. Eberhardt

    Present address: Department of Clinical Veterinary Medicine, University of Cambridge, Cambridge, CB3 0ES, UK

  4. Peter White

    Present address: CBD Porton Down, Salisbury, SP4 0JG, UK

  5. Geoffrey P. Hazlewood

    Present address: Finnfeeds International, PO Box 777, Marlborough, SN8 1XN, UK

Authors and Affiliations

  1. Department of Molecular Biology and Biotechnology, Krebs Institute, University of Sheffield, Firth Court, Western Bank, S10 2TN, Sheffield, UK

    S. Raghothama, Peter Simpson & Michael P. Williamson

  2. Laboratory of Molecular Enzymology, The Babraham Institute, Babraham, CB2 4AT, Cambridge, UK

    Ruth Y. Eberhardt, Darran Wigelsworth, Peter White & Geoffrey P. Hazlewood

  3. Department of Biological and Nutritional Sciences, University of Newcastle upon Tyne, Newcastle upon Tyne, NE1 7RU, UK

    Tibor Nagy

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Correspondence to Michael P. Williamson.

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Raghothama, S., Eberhardt, R., Simpson, P. et al. Characterization of a cellulosome dockerin domain from the anaerobic fungus Piromyces equi. Nat Struct Mol Biol 8, 775–778 (2001). https://doi.org/10.1038/nsb0901-775

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