4AZD

T57V mutant of aspartate decarboxylase

Summary for 4AZD

• Entry DOI: 10.2210/pdb4azd/pdb
• Related: 1AW8 1PPY 1PQE 1PQF 1PQH 1PT0 1PT1 1PYQ 1PYU 4AOK 4AON
• Descriptor: ASPARTATE 1-DECARBOXYLASE, MALONATE ION (3 entities in total)
• Functional Keywords: lyase, amino acid substitution
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 2
• Total formula weight: 31964.04

Authors

Webb, M.E.,Yorke, B.A.,Kershaw, T.,Lovelock, S.,Lobley, C.M.C.,Kilkenny, M.L.,Smith, A.G.,Blundell, T.L.,Pearson, A.R.,Abell, C. (deposition date: 2012-06-25, release date: 2012-07-25, Last modification date: 2023-12-20)

Primary citation

Webb, M.E.,Yorke, B.A.,Kershaw, T.,Lovelock, S.,Lobley, C.M.C.,Kilkenny, M.L.,Smith, A.G.,Blundell, T.L.,Pearson, A.R.,Abell, C.
Threonine 57 is Required for the Post-Translational Activation of Escherichia Coli Aspartate Alpha-Decarboxylase
Acta Crystallogr.,Sect.D, 70:1166-, 2014

PubMed Abstract: Aspartate α-decarboxylase is a pyruvoyl-dependent decarboxylase required for the production of β-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.

PubMed: 24699660
DOI: 10.1107/S1399004713034275

Experimental method

X-RAY DIFFRACTION (1.62 Å)