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Structure of Escherichia coli aspartate α-decarboxylase Asn72Ala: probing the role of Asn72 in pyruvoyl cofactor formation

Webb, ME, Lobley, CM, Soliman, F, Kilkenny, ML, Smith, AG, Blundell, TL and Abell, C (2012) Structure of Escherichia coli aspartate α-decarboxylase Asn72Ala: probing the role of Asn72 in pyruvoyl cofactor formation. Acta CrystallographicaSection F: Structural Biology and Crystallization Communications Online, 68 (4). 414 - 417 . ISSN 1744-3091

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Abstract

The crystal structure of the Asn72Ala site-directed mutant of Escherichia coli aspartate α-decarboxylase (ADC) has been determined at 1.7 Å resolution. The refined structure is consistent with the presence of a hydrolysis product serine in the active site in place of the pyruvoyl group required for catalysis, which suggests that the role of Asn72 is to protect the ester formed during ADC activation from hydrolysis. In previously determined structures of activated ADC, including the wild type and other site-directed mutants, the C-terminal region of the protein is disordered, but in the Asn72Ala mutant these residues are ordered owing to an interaction with the active site of the neighbouring symmetry-related multimer.

Item Type: Article
Keywords: Enzyme Activation, Escherichia coli, Glutamate Decarboxylase, Models, Molecular, Mutation, Protein Structure, Quaternary, Protein Structure, Tertiary, Substrate Specificity
Institution: The University of Leeds
Academic Units: The University of Leeds > Faculty of Maths and Physical Sciences (Leeds) > School of Chemistry (Leeds)
Depositing User: Symplectic Publications
Date Deposited: 22 Aug 2012 11:53
Last Modified: 08 Feb 2013 17:39
Published Version: http://dx.doi.org/10.1107/S1744309112009487
Status: Published
Publisher: International Union of Crystallography
Identification Number: 10.1107/S1744309112009487
URI: http://eprints.whiterose.ac.uk/id/eprint/74468

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