Please use this identifier to cite or link to this item: http://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
RMID: 0020090306
DOI: 10.1016/j.tibs.2008.11.001
Appears in Collections:Molecular and Biomedical Science publications

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