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

An ACP structural switch: conformational differences between the apo and holo forms of the actinorhodin polyketide synthase acyl carrier protein.

Chembiochem : a European journal of chemical biology - 13 Oct 2008

Evans Simon E, Williams Christopher, Arthur Christopher J, Burston Steven G, Simpson Thomas J, Crosby John, Crump Matthew P

Abstract excerpt

The actinorhodin (act) synthase acyl carrier protein (ACP) from Streptomyces coelicolor plays a central role in polyketide biosynthesis. Polyketide intermediates are bound to the free sulfhydryl group of a phosphopantetheine arm that is covalently linked to a conserved serine residue in the holo...

Read the complete abstract on PubMed

Topics

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

Share to Acyl Carrier Protein
Share to Bacillus subtilis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Holoenzymes

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Polyketide Synthases

Share to Protein Structure, Tertiary

Share to Streptomyces coelicolor

Source

Identifiers

PMID: 18770515
DOI: 10.1002/cbic.200800180

Genes

FAS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-18770515-2026-09-04.2. 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

An ACP structural switch: conformational differences between the apo and holo forms of the actinorhodin polyketide synthase acyl carrier protein.PMID 18770515Read ↗

Evidence for a protein-protein interaction motif on an acyl carrier protein domain from a modular polyketide synthase.Semantic proximity Read ↗

Genetic construction and functional analysis of hybrid polyketide synthases containing heterologous acyl carrier proteins.Semantic proximity Read ↗

Structure of acyl carrier protein bound to FabI, the FASII enoyl reductase from Escherichia coli.Semantic proximity Read ↗

Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding.Semantic proximity Read ↗

Rigidifying acyl carrier protein domain in iterative type I PKS CalE8 does not affect its function.Semantic proximity Read ↗

A bacterial acyl aminoacyl peptidase couples flexibility and stability as a result of cold adaptation.Semantic proximity Read ↗

A close look at a ketosynthase from a trans-acyltransferase modular polyketide synthase.Semantic proximity Read ↗

NMR structure of Mistic, a membrane-integrating protein for membrane protein expression.Semantic proximity Read ↗

Stability and Conformation of a Chemoreceptor HAMP Domain Chimera Correlates with Signaling Properties.Semantic proximity Read ↗

Stability and binding of the phosphorylated species of the N-terminal domain of enzyme I and the histidine phosphocarrier protein from the Streptomyces coelicolor phosphoenolpyruvate:sugar phosphotransferase system.Semantic proximity Read ↗

Identification of the structural determinants for the stability of substrate and aminoacrylate external Schiff bases in O-acetylserine sulfhydrylase-A.Semantic proximity Read ↗

Biochemical activities of the absA two-component system of Streptomyces coelicolor.Semantic proximity Read ↗

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