{
  "abstract": "Polysaccharide-degrading enzymes are generally modular proteins that contain non-catalytic carbohydrate-binding modules (CBMs), which potentiate the activity of the catalytic module. CBMs have been grouped into sequence-based families, and three-dimensional structural data are available for half of these families. Clostridium thermocellum xylanase 11A is a modular enzyme that contains a CBM from family 6 (CBM6), for which no structural data are available. We have determined the crystal structure of this module to a resolution of 2.1 A. The protein is a beta-sandwich that contains two potential ligand-binding clefts designated cleft A and B. The CBM interacts primarily with xylan, and NMR spectroscopy coupled with site-directed mutagenesis identified cleft A, containing Trp-92, Tyr-34, and Asn-120, as the ligand-binding site. The overall fold of CBM6 is similar to proteins in CBM families 4 and 22, although surprisingly the ligand-binding site in CBM4 and CBM22 is equivalent to cleft B in CBM6. These structural data define a superfamily of CBMs, comprising CBM4, CBM6, and CBM22, and demonstrate that, although CBMs have evolved from a relatively small number of ancestors, the structural elements involved in ligand recognition have been assembled at different locations on the ancestral scaffold.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 13,
  "authors": [
    {
      "name": "Mirjam Czjzek"
    },
    {
      "name": "David Bolam"
    },
    {
      "name": "Amor Mosbah"
    },
    {
      "name": "Julie Allouch"
    },
    {
      "name": "Carlos M.G.A. Fontes"
    },
    {
      "name": "Luis M.A. Ferreira"
    },
    {
      "name": "Olivier Bornet"
    },
    {
      "name": "Véronique Zamboni"
    },
    {
      "name": "Hervé Darbon"
    },
    {
      "name": "Nicola Smith"
    },
    {
      "name": "Gary Black"
    },
    {
      "name": "Bernard Henrissat"
    },
    {
      "name": "Harry Gilbert"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/fgh2zps0sn6dz.bib",
  "cited_by": 116,
  "doi": "10.1074/jbc.m109142200",
  "fulltext_url": null,
  "id": "fgh2zps0sn6dz",
  "issns": [
    "0021-9258",
    "1083-351X"
  ],
  "landing_url": "https://hal.science/hal-05797422v1",
  "language": "en",
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "journal",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "hal",
      "0.sdv"
    ],
    [
      "openalex",
      "2505|Enzyme Structure and Function"
    ]
  ],
  "openalex": "W1882486170",
  "pdf_url": "http://www.jbc.org/article/S0021925819403864/pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-13",
  "publisher": "American Society for Biochemistry and Molecular Biology",
  "ris": "https://research.draconitic.com/paper/fgh2zps0sn6dz.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:56Z",
      "native_id": "hal-05797422",
      "source": "hal",
      "url": "https://hal.science/hal-05797422v1"
    }
  ],
  "subjects": [
    {
      "field": "chemistry",
      "origin": "openalex:2505|Enzyme Structure and Function",
      "subfield": "materials-polymers"
    }
  ],
  "title": "The Location of the Ligand-binding Site of Carbohydrate-binding Modules That Have Evolved from a Common Sequence Is Not Conserved",
  "title_text": "The Location of the Ligand-binding Site of Carbohydrate-binding Modules That Have Evolved from a Common Sequence Is Not Conserved",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:17:56Z",
  "url": "https://research.draconitic.com/paper/fgh2zps0sn6dz",
  "venue": "Journal of Biological Chemistry",
  "versions": []
}