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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 form of the ACP. The solution NMR structures of both the apo and holo forms of the ACP are reported, which represents...

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Share to Acyl Carrier Protein
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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

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Identifiers

PMID: 18770515
DOI: 10.1002/cbic.200800180

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FAS

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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