Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Domain organization of the polymerizing mannosyltransferases involved in synthesis of the Escherichia coli O8 and O9a lipopolysaccharide O-antigens.

The Journal of biological chemistry - 2 Nov 2012

Greenfield Laura K, Richards Michele R, Vinogradov Evgeny, Wakarchuk Warren W, Lowary Todd L, Whitfield Chris

Abstract excerpt

The Escherichia coli O9a and O8 polymannose O-polysaccharides (O-PSs) serve as model systems for the biosynthesis of bacterial polysaccharides by ATP-binding cassette transporter-dependent pathways. Both O-PSs contain a conserved primer-adaptor domain at the reducing terminus and a serotype-speci...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Motifs
Share to Carbohydrate Sequence
Share to Escherichia coli Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Immunoblotting

Share to Magnetic Resonance Spectroscopy

Share to Mannosyltransferases

Share to O Antigens

Share to Polymerization

Source

Open in PubMed Open full text

Identifiers

PMID: 22989876
DOI: 10.1074/jbc.M112.412577
PMCID: PMC3488083

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-22989876-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Domain organization of the polymerizing mannosyltransferases involved in synthesis of the Escherichia coli O8 and O9a lipopolysaccharide O-antigens.PMID 22989876Read ↗

The C-terminal domain of the nucleotide-binding domain protein Wzt determines substrate specificity in the ATP-binding cassette transporter for the lipopolysaccharide O-antigens in Escherichia coli serotypes O8 and O9a.Semantic proximity Read ↗

Molecular insights into the assembly and diversity of the outer core oligosaccharide in lipopolysaccharides from Escherichia coli and Salmonella.Semantic proximity Read ↗

Identification of the Pseudomonas aeruginosa O17 and O15 O-Specific Antigen Biosynthesis Loci Reveals an ABC Transporter-Dependent Synthesis Pathway and Mechanisms of Genetic Diversity.Semantic proximity Read ↗

Biosynthesis of O-antigens: genes and pathways involved in nucleotide sugar precursor synthesis and O-antigen assembly.Semantic proximity Read ↗

The Klebsiella pneumoniae O12 ATP-binding Cassette (ABC) Transporter Recognizes the Terminal Residue of Its O-antigen Polysaccharide Substrate.Semantic proximity Read ↗

Structural insights into the polytopic Escherichia coli phosphoglycosyl transferase WbaP.Semantic proximity Read ↗

Structural analysis of WbpE from Pseudomonas aeruginosa PAO1: a nucleotide sugar aminotransferase involved in O-antigen assembly.Semantic proximity Read ↗

Horizontally acquired glycosyltransferase operons drive salmonellae lipopolysaccharide diversity.Semantic proximity Read ↗

Genetic loci for coaggregation receptor polysaccharide biosynthesis in Streptococcus gordonii 38.Semantic proximity Read ↗

Roles of conserved proline and glycosyltransferase motifs of EmbC in biosynthesis of lipoarabinomannan.Semantic proximity Read ↗

Structure and genetics of Escherichia coli O antigens.Semantic proximity Read ↗

Identification and characterization of six glycosyltransferases involved in the biosynthesis of a new bacterial exopolysaccharide in Paenibacillus elgii.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.