The Conformation and Function of a Multimodular Glycogen-Degrading Pneumococcal Virulence Factor
| Autor: | N.E. Warry, Uwe H. Stroeher, Mirjam Czjzek, Alisdair B. Boraston, Robert D. Burke, Benjamin Pluvinage, Lehua Deng, A. David Ogunniyi, Jan-Hendrik Hehemann, David J. Vocadlo, Elizabeth Ficko-Blean, James C. Paton, Melanie A. Higgins, Alicia Lammerts van Bueren |
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| Přispěvatelé: | van Bueren, Alicia Lammerts, Ficko-Blean, Elizabeth, Pluvinage, Benjamin, Hehemann, Jan-Hendrik, Higgins, Melanie A, Deng, Lehua, Ogunniyi, A David, Stroeher, Uwe H, El Warry, Nahida, Burke, Robert D, Czjzek, Mirjam, Paton, James C, Vocadlo, David J, Boraston, Alisdair B |
| Jazyk: | angličtina |
| Předmět: |
Models
Molecular Biochemistry & Molecular Biology Glycoside Hydrolases Protein Conformation Virulence Factors enzymes Biophysics Virulence Mice Inbred Strains Plasma protein binding SpuA Biology medicine.disease_cause Crystallography X-Ray Virulence factor Pneumococcal Infections 03 medical and health sciences Mice Protein structure Bacterial Proteins Structural Biology Cell Wall Cell Line Tumor Streptococcus pneumoniae Scattering Small Angle medicine Animals Humans Binding site Molecular Biology Gene Lung X-ray crystallography 030304 developmental biology carbohydrate binding 0303 health sciences Binding Sites 030302 biochemistry & molecular biology Cell Biology Recombinant Proteins Biochemistry Multiprotein Complexes Function (biology) Glycogen Protein Binding |
| Zdroj: | Structure. (5):640-651 |
| ISSN: | 0969-2126 |
| DOI: | 10.1016/j.str.2011.03.001 |
| Popis: | SpuA is a large multimodular cell wall-attached enzyme involved in the degradation of glycogen by the pathogenic bacterium Streptococcus pneumoniae. The deletion of the gene encoding SpuA from the bacterium resulted in a strain with reduced competitiveness in a mouse model of virulence relative to the parent strain, linking the degradation of host-glycogen to the virulence of the bacterium. Through the combined use of X-ray crystallography, small-angle X-ray scattering, and inhibitor binding, the molecular features involved in substrate recognition by this complex protein are revealed. This uniquely illustrates the complexity of the active site, the conformational changes incurred during carbohydrate binding by this protein, and the interaction and cooperation of its composite modules during this process. New insight into the function of this particular pneumococcal virulence factor is provided along with substantial contributions to the nascent framework for understanding the structural and functional interplay between modules in multimodular carbohydrate-active enzymes. Refereed/Peer-reviewed |
| Databáze: | OpenAIRE |
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