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https://hdl.handle.net/2440/45309
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Type: | Journal article |
Title: | Bacterial polysaccharide co-polymerases share a common framework for control of polymer length |
Author: | Tocilj, A. Munger, C. Proteau, A. Morona, R. Purins, L. Ajamian, E. Wagner, J. Papadopoulos, M. Van Den Bosch, L. Rubinstein, J. Fethiere, J. Matte, A. Cygler, M. |
Citation: | Nature Structural and Molecular Biology, 2008; 15(2):130-138 |
Publisher: | Nature Publishing Group |
Issue Date: | 2008 |
ISSN: | 1545-9985 1545-9985 |
Statement of Responsibility: | Ante Tocilj, Christine Munger, Ariane Proteau, Renato Morona, Leanne Purins, Eunice Ajamian, John Wagner, Magdalene Papadopoulos, Luisa Van Den Bosch, John L Rubinstein, James Féthière, Allan Matte & Miroslaw Cygler |
Abstract: | The chain length distribution of complex polysaccharides present on the bacterial surface is determined by polysaccharide co-polymerases (PCPs) anchored in the inner membrane. We report crystal structures of the periplasmic domains of three PCPs that impart substantially different chain length distributions to surface polysaccharides. Despite very low sequence similarities, they have a common protomer structure with a long central -helix extending 100 Å into the periplasm. The protomers self-assemble into bell-shaped oligomers of variable sizes, with a large internal cavity. Electron microscopy shows that one of the full-length PCPs has a similar organization as that observed in the crystal for its periplasmic domain alone. Functional studies suggest that the top of the PCP oligomers is an important region for determining polysaccharide modal length. These structures provide a detailed view of components of the bacterial polysaccharide assembly machinery. |
Keywords: | Escherichia coli O157 Salmonella typhimurium Polysaccharides, Bacterial Bacterial Proteins Escherichia coli Proteins Microscopy, Electron, Transmission Crystallography, X-Ray Amino Acid Substitution Sequence Deletion Protein Conformation Models, Molecular |
Description: | Copyright © 2008 Nature Publishing Group |
DOI: | 10.1038/nsmb.1374 |
Published version: | http://dx.doi.org/10.1038/nsmb.1374 |
Appears in Collections: | Aurora harvest 6 Molecular and Biomedical Science publications |
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