Complexity of the Ruminococcus flavefaciens cellulosome reflects an expansion in glycan recognition
| Autor: | Arun Goyal, Pedro Bule, A.S. Luis, J.P. Knox, Silvia Vidal-Melgosa, Shabir Najmudin, Pedro M. Coutinho, Catarina G. Dourado, Maja Gro Rydahl, Arnaud Baslé, Bernard Henrissat, Harry J. Gilbert, Julia Schückel, William G.T. Willats, L M A Ferreira, Immacolata Venditto, Vânia O. Fernandes, Carlos M. G. A. Fontes, Virgínia M. R. Pires |
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| Přispěvatelé: | Gilbert, Harry J., Willats, William G. T., Fontes, Carlos M. G. A., Architecture et fonction des macromolécules biologiques (AFMB), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), EU FP7 Programme under WallTraC Project [263916], Biotechnology and Biological Sciences Research Council Project [BB/K020358/1], BioStruct-X [283570], Danish Strategic Research Council, Danish Council for Independent Research, Technology and Production Sciences, GlycAct Project [FI 10-093465], Qren [30263] |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
Models
Molecular 0301 basic medicine Glycan 030106 microbiology Cellulosomes Plasma protein binding Biology Crystallography X-Ray Cellulosome 03 medical and health sciences Bacterial Proteins Polysaccharides Ruminococcus Protein–carbohydrate interactions ComputingMilieux_MISCELLANEOUS Multidisciplinary [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] carbohydrate-binding modules protein-carbohydrate interactions carbohydrate active enZYmes cellulosomes Biological Sciences Ligand (biochemistry) biology.organism_classification [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM] [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM] 030104 developmental biology Biochemistry biology.protein Function (biology) Protein Binding |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America 26 (113), 7136-7141. (2016) 'Proceedings of the National Academy of Sciences of the USA ', vol: 113, pages: 7136-7141 (2016) Proceedings of the National Academy of Sciences Proceedings of the National Academy of Sciences of the United States of America Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2016, 113 (26), pp.7136-7141. ⟨10.1073/pnas.1601558113⟩ Proceedings of the National Academy of Sciences of the United States of America, 2016, 113 (26), pp.7136-7141. ⟨10.1073/pnas.1601558113⟩ |
| ISSN: | 0027-8424 1091-6490 |
| Popis: | The breakdown of plant cell wall (PCW) glycans is an important biological and industrial process. Noncatalytic carbohydrate binding modules (CBMs) fulfill a critical targeting function in PCW depolymerization. Defining the portfolio of CBMs, the CBMome, of a PCW degrading system is central to understanding the mechanisms by which microbes depolymerize their target substrates. Ruminococcus flavefaciens, a major PCW degrading bacterium, assembles its catalytic apparatus into a large multienzyme complex, the cellulosome. Significantly, bioinformatic analyses of the R. flavefaciens cellulosome failed to identify a CBM predicted to bind to crystalline cellulose, a key feature of the CBMome of other PCW degrading systems. Here, high throughput screening of 177 protein modules of unknown function was used to determine the complete CBMome of R. flavefaciens. The data identified six previously unidentified CBMfamilies that targeted beta-glucans, beta-mannans, and the pectic polysaccharide homogalacturonan. The crystal structures of four CBMs, in conjunction with site-directed mutagenesis, provide insight into the mechanism of ligand recognition. In the CBMs that recognize beta-glucans and beta-mannans, differences in the conformation of conserved aromatic residues had a significant impact on the topology of the ligand binding cleft and thus ligand specificity. A cluster of basic residues in CBM77 confers calcium-independent recognition of homogalacturonan, indicating that the carboxylates of galacturonic acid are key specificity determinants. This report shows that the extended repertoire of proteins in the cellulosome of R. flavefaciens contributes to an extended CBMome that supports efficient PCW degradation in the absence of CBMs that specifically target crystalline cellulose. |
| Databáze: | OpenAIRE |
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