ArticleBiophysical journal2005
Protein disorder: conformational distribution of the flexible linker in a chimeric double cellulase.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- The Effect of CBM1 and Linker on the Oxidase, Peroxidase and Monooxygenase Activities of AA9 LPMOs: Insight into Their Correlation with the Nature of Reductants and Crystallinity of Celluloses.International journal of molecular sciences · 2024Article
- Sas20 is a highly flexible starch-binding protein in the Ruminococcus bromii cell-surface amylosome.The Journal of biological chemistry · 2022Article
- The diversity of molecular interactions involving intrinsically disordered proteins: A molecular modeling perspective.Computational and structural biotechnology journal · 2021Review
- Intrinsically Disordered Linkers Impart Processivity on Enzymes by Spatial Confinement of Binding Domains.International journal of molecular sciences · 2019Article
- Dual binding in cohesin-dockerin complexes: the energy landscape and the role of short, terminal segments of the dockerin module.Scientific reports · 2018Article
- Distinct roles of N- and O-glycans in cellulase activity and stability.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- CCProf: exploring conformational change profile of proteins.Database : the journal of biological databases and curation · 2016Article
- Functional Characterization and Low-Resolution Structure of an Endoglucanase Cel45A from the Filamentous Fungus Neurospora crassa OR74A: Thermostable Enzyme with High Activity Toward Lichenan and β-Glucan.Molecular biotechnology · 2015Article
- Advances in Understanding Carboxysome Assembly in Prochlorococcus and Synechococcus Implicate CsoS2 as a Critical Component.Life (Basel, Switzerland) · 2015Article
- Multifunctional cellulase catalysis targeted by fusion to different carbohydrate-binding modules.Biotechnology for biofuels · 2015Article
- Article
- Structural disorder provides increased adaptability for vesicle trafficking pathways.PLoS computational biology · 2013Article
- X-ray crystal structure of the streptococcal specific phage lysin PlyC.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- New developments in theJournal of applied crystallography · 2012Article
- How random are intrinsically disordered proteins? A small angle scattering perspective.Current protein & peptide science · 2012Review
- Understanding the structural ensembles of a highly extended disordered protein.Molecular bioSystems · 2012Article
- Antitumoral activity of allosteric inhibitors of protein kinase CK2.Oncotarget · 2011Article
- X-ray solution scattering studies of the structural diversity intrinsic to protein ensembles.Biopolymers · 2011Article
- The O-glycosylated linker from the Trichoderma reesei Family 7 cellulase is a flexible, disordered protein.Biophysical journal · 2010Article
- Effect of linker length and dockerin position on conversion of a Thermobifida fusca endoglucanase to the cellulosomal mode.Applied and environmental microbiology · 2009Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
The structural properties of the linker peptide connecting the cellulose-binding module to the catalytic module in bimodular cellulases have been investigated by small-angle x-ray scattering. Since the linker and the cellulose-binding module are relatively small and cannot be readily detected separately, the conformation of the linker was studied by means of an artificial fusion protein, Cel6BA, in which an 88-residue linker connects the large catalytic modules of the cellulases Cel6A and Cel6B from Humicola insolens. Our data showed that Cel6BA is very elongated with a maximum dimension of 178 A, but could not be described by a single conformation. Modeling of a series of Cel6BA conformers with interdomain separations ranging between 10 A and 130 A showed that good Guinier and P(r) profile fits were obtained by a weighted average of the scattering curves of all the models where the linker follows a nonrandom distribution, with a preference for the more compact conformers. These structural properties are likely to be essential for the function of the linker as a molecular spring between the two functional modules. Small-angle x-ray scattering therefore provides a unique tool to quantitatively analyze the conformational disorder typical of proteins described as natively unfolded.
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