{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Dorival J"],"funding":["FP7 Nanosciences, Nanotechnologies, Materials and new Production Technologies","Narodowym Centrum Nauki","ADEME ERANET IB"],"pagination":["68"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9210761"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_abstract":["<h4>Background</h4>Natural cellulosome multi-enzyme complexes, their components, and engineered 'designer cellulosomes' (DCs) promise an efficient means of breaking down cellulosic substrates into valuable biofuel products. Their broad uptake in biotechnology relies on boosting proximity-based synergy among the resident enzymes, but the modular architecture challenges structure determination and rational design.<h4>Results</h4>We used small angle X-ray scattering combined with molecular modeling to study the solution structure of cellulosomal components. These include three dockerin-bearing cellulases with distinct substrate specificities, original scaffoldins from the human gut bacterium Ruminococcus champanellensis (ScaA, ScaH and ScaK) and a trivalent cohesin-bearing designer scaffoldin"],"journal":["Biotechnology for biofuels and bioproducts"],"pubmed_title":["Mapping the deformability of natural and designed cellulosomes in solution."],"pmcid":["PMC9210761"],"funding_grant_id":["2016/21/B/NZ1/00006","1201C0104","604530"],"pubmed_authors":["Morais S","Dabin J","Rozycki B","Cazade PA","Thureau A","Czjzek M","Dorival J","Labourel A","Bayer EA","Setter-Lamed E","Mizrahi I","Thompson D"],"additional_accession":[]},"is_claimable":false,"name":"Mapping the deformability of natural and designed cellulosomes in solution.","description":"<h4>Background</h4>Natural cellulosome multi-enzyme complexes, their components, and engineered 'designer cellulosomes' (DCs) promise an efficient means of breaking down cellulosic substrates into valuable biofuel products. Their broad uptake in biotechnology relies on boosting proximity-based synergy among the resident enzymes, but the modular architecture challenges structure determination and rational design.<h4>Results</h4>We used small angle X-ray scattering combined with molecular modeling to study the solution structure of cellulosomal components. These include three dockerin-bearing cellulases with distinct substrate specificities, original scaffoldins from the human gut bacterium Ruminococcus champanellensis (ScaA, ScaH and ScaK) and a trivalent cohesin-bearing designer scaffoldin","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jun","modification":"2026-05-10T02:11:43.829Z","creation":"2024-11-09T18:57:10.612Z"},"accession":"S-EPMC9210761","cross_references":{"pubmed":["35725490"],"doi":["10.1186/s13068-022-02165-3"]}}