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Here, by solving the crystal structure, it is shown that\n                    <jats:italic>Mt<\/jats:italic>\n                    Glu5 from\n                    <jats:italic>Meiothermus taiwanensis<\/jats:italic>\n                    WR-220, a GH5-family endo-\u03b2-1,4-glucanase (EC 3.2.1.4), has a bipartite architecture consisting of a Cel5A-like catalytic domain with a (\u03b2\/\u03b1)\n                    <jats:sub>8<\/jats:sub>\n                    TIM-barrel fold and an inserted CBM29-like noncatalytic domain with a \u03b2-jelly-roll fold. Deletion of the CBM significantly reduced the catalytic efficiency of\n                    <jats:italic>Mt<\/jats:italic>\n                    Glu5, as determined by isothermal titration calorimetry using inactive mutants of full-length and CBM-deleted\n                    <jats:italic>Mt<\/jats:italic>\n                    Glu5 proteins. Conversely, insertion of the CBM from\n                    <jats:italic>Mt<\/jats:italic>\n                    Glu5 into\n                    <jats:italic>Tm<\/jats:italic>\n                    Cel5A from\n                    <jats:italic>Thermotoga maritima<\/jats:italic>\n                    greatly enhanced the substrate affinity of\n                    <jats:italic>Tm<\/jats:italic>\n                    Cel5A. Bound sugars observed between two tryptophan side chains in the catalytic domains of active full-length and CBM-deleted\n                    <jats:italic>Mt<\/jats:italic>\n                    Glu5 suggest an important stacking force. The synergistic action of the catalytic domain and CBM of\n                    <jats:italic>Mt<\/jats:italic>\n                    Glu5 in binding to single-chain polysaccharides was visualized by substrate modeling, in which additional surface tryptophan residues were identified in a cross-domain groove. Subsequent site-specific mutagenesis results confirmed the pivotal role of several other tryptophan residues from both domains of\n                    <jats:italic>Mt<\/jats:italic>\n                    Glu5 in substrate binding. These findings reveal a way to incorporate a CBM into the catalytic domain of an existing enzyme to make a robust cellulase.\n                  <\/jats:p>","DOI":"10.1107\/s2059798322002601","type":"journal-article","created":{"date-parts":[[2022,4,20]],"date-time":"2022-04-20T10:40:51Z","timestamp":1650451251000},"page":"633-646","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":15,"title":["Synergic action of an inserted carbohydrate-binding module in a glycoside hydrolase family 5 endoglucanase"],"prefix":"10.1107","volume":"78","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5795-5815","authenticated-orcid":true,"given":"Ting-Juan","family":"Ye","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/05bxb3784","id-type":"ROR","asserted-by":"publisher"}],"department":["Institute of Biological Chemistry"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5235-7421","authenticated-orcid":true,"given":"Kai-Fa","family":"Huang","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/05bxb3784","id-type":"ROR","asserted-by":"publisher"}],"department":["Institute of Biological Chemistry"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1794-2638","authenticated-orcid":true,"given":"Tzu-Ping","family":"Ko","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/05bxb3784","id-type":"ROR","asserted-by":"publisher"}],"department":["Institute of Biological Chemistry"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shih-Hsiung","family":"Wu","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/05bxb3784","id-type":"ROR","asserted-by":"publisher"}],"department":["Institute of Biological Chemistry"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"329","published-online":{"date-parts":[[2022,4,20]]},"reference":[{"key":"jc5049_bb1","doi-asserted-by":"crossref","first-page":"18496","DOI":"10.1073\/pnas.0706443104","volume":"104","author":"Arora","year":"2007","journal-title":"Proc. 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