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

Functional analysis of the large periplasmic loop of the Escherichia coli K-12 WaaL O-antigen ligase.

Molecular microbiology - 1 Dec 2008

Pérez José M, McGarry Megan A, Marolda Cristina L, Valvano Miguel A

Abstract excerpt

WaaL is a membrane enzyme implicated in ligating undecaprenyl-diphosphate (Und-PP)-linked O antigen to lipid A-core oligosaccharide. We determined the periplasmic location of a large (EL5) and small (EL4) adjacent loops in the Escherichia coli K-12 WaaL. Structural models of the EL5 from the K-12...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Carbon-Oxygen Ligases
Share to Conserved Sequence

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli Proteins

Share to Green Fluorescent Proteins

Share to Ligases

Share to Periplasm

Share to Recombinant Fusion Proteins

Source

Identifiers

PMID: 19019161
DOI: 10.1111/j.1365-2958.2008.06490.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19019161-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional analysis of the large periplasmic loop of the Escherichia coli K-12 WaaL O-antigen ligase.PMID 19019161Read ↗

Investigation of the structural requirements in the lipopolysaccharide core acceptor for ligation of O antigens in the genus Salmonella: WaaL "ligase" is not the sole determinant of acceptor specificity.Semantic proximity Read ↗

Molecular and functional characterization of O antigen transfer in Vibrio cholerae.Semantic proximity Read ↗

Defining function of lipopolysaccharide O-antigen ligase WaaL using chemoenzymatically synthesized substrates.Semantic proximity Read ↗

Functional characterization of WaaL, a ligase associated with linking O-antigen polysaccharide to the core of Pseudomonas aeruginosa lipopolysaccharide.Semantic proximity Read ↗

A mutant Escherichia coli that attaches peptidoglycan to lipopolysaccharide and displays cell wall on its surface.Semantic proximity Read ↗

Periplasmic protein-protein contacts in the inner membrane protein Wzc form a tetrameric complex required for the assembly of Escherichia coli group 1 capsules.Semantic proximity Read ↗

Crystal structures of two bacterial HECT-like E3 ligases in complex with a human E2 reveal atomic details of pathogen-host interactionsSemantic proximity Read ↗

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

Translocation of group 1 capsular polysaccharide in Escherichia coli serotype K30. Structural and functional analysis of the outer membrane lipoprotein Wza.Semantic proximity Read ↗

Structural and functional characterization of VanG D-Ala:D-Ser ligase associated with vancomycin resistance in Enterococcus faecalis.Semantic proximity Read ↗

A catalytically essential motif in external loop 5 of the bacterial oligosaccharyltransferase PglB.Semantic proximity Read ↗

Induced-fit motion of a lid loop involved in catalysis in alginate lyase A1-III.Semantic proximity Read ↗

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