{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,18]],"date-time":"2026-03-18T21:01:18Z","timestamp":1773867678145,"version":"3.50.1"},"reference-count":42,"publisher":"Proceedings of the National Academy of Sciences","issue":"9","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2007,2,27]]},"abstract":"<jats:p>\n            The assembly of proteins that display complementary activities into macromolecular complexes is critical to cellular function. One such enzyme complex, of environmental significance, is the plant cell wall degrading apparatus of anaerobic bacteria, termed the cellulosome. The complex assembles through the interaction of enzyme-derived \u201ctype I dockerin\u201d modules with the multiple \u201ccohesin\u201d modules of the scaffolding protein.\n            <jats:italic>Clostridium thermocellum<\/jats:italic>\n            type I dockerin modules contain a duplicated 22-residue sequence that comprises helix-1 and helix-3, respectively. The crystal structure of a\n            <jats:italic>C. thermocellum<\/jats:italic>\n            type I cohesin-dockerin complex showed that cohesin recognition was predominantly through helix-3 of the dockerin. The sequence duplication is reflected in near-perfect 2-fold structural symmetry, suggesting that both repeats could interact with cohesins by a common mechanism in wild-type (WT) proteins. Here, a helix-3 disrupted mutant dockerin is used to visualize the reverse binding in which the dockerin mutant is indeed rotated 180\u00b0 relative to the WT dockerin such that helix-1 now dominates recognition of its protein partner. The dual binding mode is predicted to impart significant plasticity into the orientation of the catalytic subunits within this supramolecular assembly, which reflects the challenges presented by the degradation of a heterogeneous, recalcitrant, insoluble substrate by a tethered macromolecular complex.\n          <\/jats:p>","DOI":"10.1073\/pnas.0611173104","type":"journal-article","created":{"date-parts":[[2007,2,21]],"date-time":"2007-02-21T05:04:11Z","timestamp":1172034251000},"page":"3089-3094","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":135,"title":["Evidence for a dual binding mode of dockerin modules to cohesins"],"prefix":"10.1073","volume":"104","author":[{"given":"Ana Lu\u00edsa","family":"Carvalho","sequence":"first","affiliation":[{"name":"*Rede de Qu\u00edmica e Tecnologia\/Centro de Qu\u00edmica Fina e Biotecnologia (REQUIMTE\/CQFB), Departamento de Qu\u00edmica, Faculdade de Ci\u00eancias e Tecnologia, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal;"}]},{"given":"Fernando M. V.","family":"Dias","sequence":"additional","affiliation":[{"name":"Centro Interdisciplinar de Investiga\u00e7\u00e3o em Sanidade Animal Faculdade de Medicina Veterin\u00e1ria, Universidade T\u00e9cnica de Lisboa, Avenida da Universidade T\u00e9cnica, 1300-477 Lisbon, Portugal;"}]},{"given":"Tibor","family":"Nagy","sequence":"additional","affiliation":[{"name":"Institute for Cell and Molecular Biosciences, University of Newcastle upon Tyne, The Medical School, Newcastle upon Tyne NE2 4HH, United Kingdom;"}]},{"given":"Jos\u00e9 A. M.","family":"Prates","sequence":"additional","affiliation":[{"name":"Centro Interdisciplinar de Investiga\u00e7\u00e3o em Sanidade Animal Faculdade de Medicina Veterin\u00e1ria, Universidade T\u00e9cnica de Lisboa, Avenida da Universidade T\u00e9cnica, 1300-477 Lisbon, Portugal;"}]},{"given":"Mark R.","family":"Proctor","sequence":"additional","affiliation":[{"name":"Institute for Cell and Molecular Biosciences, University of Newcastle upon Tyne, The Medical School, Newcastle upon Tyne NE2 4HH, United Kingdom;"}]},{"given":"Nicola","family":"Smith","sequence":"additional","affiliation":[{"name":"Institute for Cell and Molecular Biosciences, University of Newcastle upon Tyne, The Medical School, Newcastle upon Tyne NE2 4HH, United Kingdom;"}]},{"given":"Edward A.","family":"Bayer","sequence":"additional","affiliation":[{"name":"Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel; and"}]},{"given":"Gideon J.","family":"Davies","sequence":"additional","affiliation":[{"name":"Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5YW, United Kingdom"}]},{"given":"Lu\u00eds M. A.","family":"Ferreira","sequence":"additional","affiliation":[{"name":"Centro Interdisciplinar de Investiga\u00e7\u00e3o em Sanidade Animal Faculdade de Medicina Veterin\u00e1ria, Universidade T\u00e9cnica de Lisboa, Avenida da Universidade T\u00e9cnica, 1300-477 Lisbon, Portugal;"}]},{"given":"Maria J.","family":"Rom\u00e3o","sequence":"additional","affiliation":[{"name":"*Rede de Qu\u00edmica e Tecnologia\/Centro de Qu\u00edmica Fina e Biotecnologia (REQUIMTE\/CQFB), Departamento de Qu\u00edmica, Faculdade de Ci\u00eancias e Tecnologia, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal;"}]},{"given":"Carlos M. G. 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