Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 23117123Publication DOI: 10.1016/j.tim.2012.10.001Journal NLM ID: 9310916Publisher: Cambridge: Elsevier Trends Journals
Correspondence: Howell PL <howell
sickkids.ca>
Institutions: Program in Molecular Structure and Function, The Hospital for Sick Children, 555 University Avenue, Toronto, ON M5G 1X8, Canada
The biosynthesis and export of bacterial cell-surface polysaccharides is known to occur through several distinct mechanisms. Recent advances in the biochemistry and structural biology of several proteins in synthase-dependent polysaccharide secretion systems have identified key conserved components of this pathway in Gram-negative bacteria. These components include an inner-membrane-embedded polysaccharide synthase, a periplasmic tetratricopeptide repeat (TPR)-containing scaffold protein, and an outer-membrane beta-barrel porin. There is also increasing evidence that many synthase-dependent systems are post-translationally regulated by the bacterial second messenger bis-(3'-5')-cyclic dimeric guanosine monophosphate (c-di-GMP). Here, we compare these core proteins in the context of the alginate, cellulose, and poly-β-D-N-acetylglucosamine (PNAG) secretion systems.
exopolysaccharide, alginate, cellulose, synthase, poly-β-D-N-acetylglucosamine
Structure type: homopolymer
Location inside paper: p.64
Trivial name: poly-β-1,6-GlcNAc (PGA), biofilm, poly-b-(1-6)-N-acetyl-D-glucosamine (PNAG), poly-β-N-acetyl-glucosamine (PNAG), PNAG, poly-N-acetylglucosamine, PNAG
Compound class: CPS, EPS, O-polysaccharide, glucan, polysaccharide
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_753248
Comments, role: review
Related record ID(s): 29812, 29813, 29814
NCBI Taxonomy refs (TaxIDs): 562Reference(s) to other database(s): GTC:G36952FI, GlycomeDB:
11210
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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