3tm7 | pdb_00003tm7

Processed Aspartate Decarboxylase Mutant with Asn72 mutated to Ala

spinqualitylabelsall models 3tm7, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3tm7 is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Related: 1aw8, 1ppy, 1pqe, 1pqf, 1pqh, 1pyq Gene: b0131, JW0127, panD (Escherichia coli) Activity: Aspartate 1-decarboxylase, with EC number 4.1.1.11 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed The crystal structure of the Asn72Ala site-directed mutant of Escherichia coli aspartate alpha-decarboxylase (ADC) has been determined at 1.7 A 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. Structure of Escherichia coli aspartate alpha-decarboxylase Asn72Ala: probing the role of Asn72 in pyruvoyl cofactor formation.,Webb ME, Lobley CM, Soliman F, Kilkenny ML, Smith AG, Blundell TL, Abell C Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Apr 1;68(Pt 4):414-7. Epub, 2012 Mar 28. PMID:22505409 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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