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Article

Crystal structure of a PCP/Sfp complex reveals the structural basis for carrier protein posttranslational modification.

Chemistry & biology - 24 Apr 2014

Tufar Peter, Rahighi Simin, Kraas Femke I, Kirchner Donata K, Löhr Frank, Henrich Erik, Köpke Jürgen, Dikic Ivan, Güntert Peter, Marahiel Mohamed A, Dötsch Volker

Abstract excerpt

Phosphopantetheine transferases represent a class of enzymes found throughout all forms of life. From a structural point of view, they are subdivided into three groups, with transferases from group II being the most widespread. They are required for the posttranslational modification of carrier proteins involved in diverse metabolic pathways. We determined the crystal structure of the group II phosphopantetheine...

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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

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Share to Crystallography, X-Ray

Share to Hydrophobic and Hydrophilic Interactions

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Share to Protein Processing, Post-Translational

Share to Transferases (Other Substituted Phosphate Groups)

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Identifiers

PMID: 24704508
DOI: 10.1016/j.chembiol.2014.02.014

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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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