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Threonine 57 is required for the post-translational activation of

DOI: 10.1107/S1399004713034275 DOI Help
PMID: 24699660 PMID Help

Authors: Michael Webb (Astbury Centre for Structural Molecular Biology, University of Leeds) , Briony Yorke (Astbury Centre for Structural Molecular Biology, University of Leeds) , Tom Kershaw (Department of Biochemistry, University of Cambridge) , Sarah Lovelock (School of Chemistry, University of Leeds) , Carina Lobley (Diamond Light Source) , Mairi Kilkenny (Department of Biochemistry, University of Cambridge) , Alison G. Smith (Department of Plant Sciences, University of Cambridge) , Tom L. Blundell (Department of Biochemistry, University of Cambridge) , Arwen Pearson (Astbury Centre for Structural Molecular Biology, University of Leeds) , Chris Abell (University Chemical Laboratory, University of Cambridge)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section D Biological Crystallography , VOL 70 , PAGES 1166 - 1172

State: Published (Approved)
Published: April 2014

Abstract: Aspartate [alpha]-decarboxylase is a pyruvoyl-dependent decarboxylase required for the production of [beta]-alanine in the bacterial pantothenate (vitamin B5) biosynthesis pathway. The pyruvoyl group is formed via the intramolecular rearrangement of a serine residue to generate a backbone ester intermediate which is cleaved to generate an N-terminal pyruvoyl group. Site-directed mutagenesis of residues adjacent to the active site, including Tyr22, Thr57 and Tyr58, reveals that only mutation of Thr57 leads to changes in the degree of post-translational activation. The crystal structure of the site-directed mutant T57V is consistent with a non-rearranged backbone, supporting the hypothesis that Thr57 is required for the formation of the ester intermediate in activation.

Subject Areas: Biology and Bio-materials, Chemistry

Facility: ESRF

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