Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/66251
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Type: Journal article
Title: The conformation and function of a multimodular glycogen-degrading pneumococcal virulence factor
Author: van Bueren, A.
Ficko-Blean, E.
Pluvinage, B.
Hehemann, J.
Higgins, M.
Deng, L.
Ogunniyi, A.
Stroeher, U.
El Warry, N.
Burke, R.
Czjzek, M.
Paton, J.
Vocadlo, D.
Boraston, A.
Citation: Structure, 2011; 19(5):640-651
Publisher: Cell Press
Issue Date: 2011
ISSN: 0969-2126
1878-4186
Statement of
Responsibility: 
Alicia Lammerts van Bueren, Elizabeth Ficko-Blean, Benjamin Pluvinage, Jan-Hendrik Hehemann, Melanie A. Higgins, Lehua Deng, A. David Ogunniyi, Uwe H. Stroeher, Nahida E Warry, Robert D. Burke, Mirjam Czjzek, James C. Paton, David J. Vocadlo and Alisdair B. Boraston
Abstract: 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.
Keywords: Lung; Cell Line, Tumor; Cell Wall; Animals; Mice, Inbred Strains; Humans; Mice; Streptococcus pneumoniae; Pneumococcal Infections; Multiprotein Complexes; Glycogen; Glycoside Hydrolases; Bacterial Proteins; Recombinant Proteins; Virulence Factors; Crystallography, X-Ray; Virulence; Binding Sites; Protein Conformation; Protein Binding; Models, Molecular; Scattering, Small Angle
Rights: Copyright © 2011 Elsevier Ltd. All rights reserved.
RMID: 0020110966
DOI: 10.1016/j.str.2011.03.001
Appears in Collections:Molecular and Biomedical Science publications

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