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

How the MccB bacterial ancestor of ubiquitin E1 initiates biosynthesis of the microcin C7 antibiotic.

The EMBO journal - 8 Jul 2009

Regni Catherine A, Roush Rebecca F, Miller Darcie J, Nourse Amanda, Walsh Christopher T, Schulman Brenda A

Abstract excerpt

The 39-kDa Escherichia coli enzyme MccB catalyses a remarkable posttranslational modification of the MccA heptapeptide during the biosynthesis of microcin C7 (MccC7), a 'Trojan horse' antibiotic. The approximately 260-residue C-terminal region of MccB is homologous to ubiquitin-like protein (UBL) activating enzyme (E1) adenylation domains. Accordingly, MccB-catalysed C-terminal MccA-acyl-adenylation is...

Read the complete abstract on PubMed

Topics

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

Share to Aspartic Acid
Share to Bacteriocins
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Ligases

Share to Nucleotides

Share to Protein Processing, Post-Translational

Share to Ubiquitin-Activating Enzymes

Source

Open in PubMed Open full text

Identifiers

PMID: 19494832
DOI: 10.1038/emboj.2009.146
PMCID: PMC2711183

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

How the MccB bacterial ancestor of ubiquitin E1 initiates biosynthesis of the microcin C7 antibiotic.PMID 19494832Read ↗

Enzymatic Synthesis and Functional Characterization of Bioactive Microcin C-Like Compounds with Altered Peptide Sequence and Length.Semantic proximity Read ↗

Structure and function of a serine carboxypeptidase adapted for degradation of the protein synthesis antibiotic microcin C7.Semantic proximity Read ↗

Systematic structure-activity analysis of microcin J25.Semantic proximity Read ↗

Escherichia coli peptidase A, B, or N can process translation inhibitor microcin C.Semantic proximity Read ↗

Insights into the biosynthesis and stability of the lasso peptide capistruin.Semantic proximity Read ↗

Sequence diversity in the lasso peptide framework: discovery of functional microcin J25 variants with multiple amino acid substitutions.Semantic proximity Read ↗

Structure and organization of plasmid genes required to produce the translation inhibitor microcin C7.Semantic proximity Read ↗

Evolutionary and functional analysis of an NRPS condensation domain integrates β-lactam, ᴅ-amino acid, and dehydroamino acid synthesisSemantic proximity Read ↗

Bifunctional quorum-quenching and antibiotic-acylase MacQ forms a 170-kDa capsule-shaped molecule containing spacer polypeptides.Semantic proximity Read ↗

Characterization of a dual function macrocyclase enables design and use of efficient macrocyclization substrates.Semantic proximity Read ↗

Class IIb Microcin MccM Interferes with Oxidative Phosphorylation in Escherichia coliSemantic proximity Read ↗

Structure of Microcin B-Like Compounds Produced by Pseudomonas syringae and Species Specificity of Their Antibacterial ActionSemantic proximity Read ↗

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