4azd

T57V mutant of aspartate decarboxylase

spinqualitylabelsall models 4azd, resolution 1.62Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4azd is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.62Å Ligands: MLI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PAND_ECOLI Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. Publication Abstract from PubMed 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. Threonine 57 is required for the post-translational activation of Escherichia coli aspartate alpha-decarboxylase.,Webb ME, Yorke BA, Kershaw T, Lovelock S, Lobley CM, Kilkenny ML, Smith AG, Blundell TL, Pearson AR, Abell C Acta Crystallogr D Biol Crystallogr. 2014 Apr 1;70(Pt 4):1166-72. doi:, 10.1107/S1399004713034275. Epub 2014 Mar 21. PMID:24699660 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aspartate decarboxylase 3D structures Beta-N-acetylhexosaminidase 3D structures

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