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

The crystal structure of two macrolide glycosyltransferases provides a blueprint for host cell antibiotic immunity.

Proceedings of the National Academy of Sciences of the United States of America - 27 Mar 2007

Bolam David N, Roberts Shirley, Proctor Mark R, Turkenburg Johan P, Dodson Eleanor J, Martinez-Fleites Carlos, Yang Min, Davis Benjamin G, Davies Gideon J, Gilbert Harry J

Abstract excerpt

Glycosylation of macrolide antibiotics confers host cell immunity from endogenous and exogenous agents. The Streptomyces antibioticus glycosyltransferases, OleI and OleD, glycosylate and inactivate oleandomycin and diverse macrolides including erythromycin, respectively. The structure of these enzyme-ligand complexes, in tandem with kinetic analysis of site-directed variants, provide insight into the interaction...

Read the complete abstract on PubMed

Topics

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

Share to Crystallography, X-Ray
Share to Drug Resistance, Bacterial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glucosyltransferases

Share to Glycosyltransferases

Share to Macrolides

Share to Models, Chemical

Share to Molecular Conformation

Share to Streptomyces

Source

Open in PubMed Open full text

Identifiers

PMID: 17376874
DOI: 10.1073/pnas.0607897104
PMCID: PMC1838483

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The crystal structure of two macrolide glycosyltransferases provides a blueprint for host cell antibiotic immunity.PMID 17376874Read ↗

Hydration and hydrolysis define antibiotic resistance conferred by macrolide esterasesSemantic proximity Read ↗

Macrolide antibiotic interaction and resistance on the bacterial ribosome.Semantic proximity Read ↗

Midecamycin Is Inactivated by Several Different Sugar Moieties at Its Inactivation Site.Semantic proximity Read ↗

Context-specific action of macrolide antibiotics on the eukaryotic ribosome.Semantic proximity Read ↗

Ribosome-binding and anti-microbial studies of the mycinamicins, 16-membered macrolide antibiotics from Micromonospora griseorubidaSemantic proximity Read ↗

Regulation of the macrolide resistance ABC-F translation factor MsrDSemantic proximity Read ↗

Avilamycin and evernimicin induce structural changes in rProteins uL16 and CTC that enhance the inhibition of A-site tRNA binding.Semantic proximity Read ↗

Two glycosyltransferases and a glycosidase are involved in oleandomycin modification during its biosynthesis by <i>Streptomyces antibioticus</i>Semantic proximity Read ↗

The structures of four macrolide antibiotics bound to the large ribosomal subunit.Semantic proximity Read ↗

Regulation of the macrolide resistance ABC-F translation factor MsrDSemantic proximity Read ↗

Precursor Directed Biosynthesis of an Orthogonally Functional Erythromycin Analogue: Selectivity in the Ribosome Macrolide Binding PocketSemantic proximity Read ↗

Stepwise binding of tylosin and erythromycin to Escherichia coli ribosomes, characterized by kinetic and footprinting analysis.Semantic proximity Read ↗

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