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https://hdl.handle.net/2440/52650
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Type: | Journal article |
Title: | Sequence-structure relationships in polysaccharide co-polymerase (PCP) proteins |
Author: | Morona, R. Purins, L. Tocilj, A. Matte, A. Cygler, M. |
Citation: | Trends in Biochemical Sciences, 2009; 34(2):78-84 |
Publisher: | Elsevier Science London |
Issue Date: | 2009 |
ISSN: | 0968-0004 |
Statement of Responsibility: | Renato Morona, Leanne Purins, Ante Tocilj, Allan Matte and Miroslaw Cygler |
Abstract: | Polysaccharides are ubiquitously distributed on the cell surface of bacteria. These polymers are involved in many processes, including immune avoidance and bacteria–host interactions, which are especially important for pathogenic organisms. In many instances, the lengths of these polysaccharides are not random, but rather distribute around some mean value, termed the modal length. A large family of proteins, called polysaccharide co-polymerases (PCPs), found in both Gram-negative and Gram-positive species regulate polysaccharide modal length. Recent crystal structures of Wzz proteins from Escherichia coli and Salmonella typhimurium provide the first atomic-resolution information for one family of PCPs, the PCP1 group. These crystal structures have important implications for the structures of other PCP families. |
Keywords: | Escherichia coli Salmonella typhimurium Polysaccharides Bacterial Proteins Crystallography, X-Ray Amino Acid Sequence Protein Conformation Genes, Bacterial Models, Molecular |
DOI: | 10.1016/j.tibs.2008.11.001 |
Published version: | http://dx.doi.org/10.1016/j.tibs.2008.11.001 |
Appears in Collections: | Aurora harvest 5 Molecular and Biomedical Science publications |
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