2YA0
Catalytic Module of the Multi-modular glycogen-degrading pneumococcal virulence factor SpuA
Summary for 2YA0
Entry DOI | 10.2210/pdb2ya0/pdb |
Related | 2J44 2YA1 2YA2 |
Descriptor | PUTATIVE ALKALINE AMYLOPULLULANASE, CALCIUM ION, GLYCEROL, ... (5 entities in total) |
Functional Keywords | hydrolase, glycoside hydrolase |
Biological source | STREPTOCOCCUS PNEUMONIAE |
Total number of polymer chains | 1 |
Total formula weight | 80898.12 |
Authors | Lammerts van Bueren, A.,Ficko-Blean, E.,Pluvinage, B.,Hehemann, J.H.,Higgins, M.A.,Deng, L.,Ogunniyi, A.D.,Stroeher, U.H.,Warry, N.E.,Burke, R.D.,Czjzek, M.,Paton, J.C.,Vocadlo, D.J.,Boraston, A.B. (deposition date: 2011-02-17, release date: 2011-04-20, Last modification date: 2023-12-20) |
Primary citation | Lammerts Van Bueren, A.,Ficko-Blean, E.,Pluvinage, B.,Hehemann, J.,Higgins, M.A.,Deng, L.,Ogunniyi, A.D.,Stroeher, U.H.,El Warry, N.,Burke, R.D.,Czjzek, M.,Paton, J.C.,Vocadlo, D.J.,Boraston, A.B. The Conformation and Function of a Multimodular Glycogen-Degrading Pneumococcal Virulence Factor. Structure, 19:640-, 2011 Cited by PubMed 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. PubMed: 21565699DOI: 10.1016/J.STR.2011.03.001 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
Download full validation report
