Modelling of the lignin peroxidase LIII of Phlebia radiata: Use of a sequence template generated from a 3-D structure

Anna-Marja Hoffren (Corresponding Author), Markku Saloheimo, Pamela Thomas, John Overington, Mark Johnson, Jonathan Knowles, Tom Blundell

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    3 Citations (Scopus)


    A model of the lignin peroxidase LIII of Phlebia radiata was constructed on the basis of the structure of cytochrome c peroxidase (CCP). Because of the low percentage of amino acid identity between the CCP and the lignin peroxidase LIII of Phlebia radiata, alignment of the sequences was based on the generation of a template from a knowledge of the 3-D structure of CCP and consensus sequences of lignin peroxidases. This approach gave an alignment in which all the insertions in the lignin peroxidase were placed at loop regions of CCP, with a 21.1% identity for these two proteins. The model was constructed using this alignment and the computer program COMPOSER, which assembles the model as a series of rigid fragments derived from CCP and other proteins. Manual intervention was required for some of the longer loop regions. The α-helices forming the structural framework, and especially the haem environment of CCP, are conserved in the LIII model and the core is close packed without holes. A possible site of the substrate oxidation at the haem edge of LIII is discussed.

    Original languageEnglish
    Pages (from-to)177 - 182
    Number of pages6
    JournalProtein Engineering
    Issue number2
    Publication statusPublished - 1993
    MoE publication typeA1 Journal article-refereed


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