3TM7

Processed Aspartate Decarboxylase Mutant with Asn72 mutated to Ala

3TM7 の概要

• エントリーDOI: 10.2210/pdb3tm7/pdb
• 関連するPDBエントリー: 1AW8 1PPY 1PQE 1PQF 1PQH 1PYQ
• 分子名称: Aspartate 1-decarboxylase beta chain, Aspartate 1-decarboxylase alpha chain, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: auto-processing, lyase, pyruvoyl
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 28131.79

構造登録者

Webb, M.E.,Lobley, C.M.C.,Soliman, F.,Kilkenny, M.L.,Smith, A.G.,Abell, C.,Blundell, T.L. (登録日: 2011-08-31, 公開日: 2012-04-11, 最終更新日: 2024-02-28)

主引用文献

Webb, M.E.,Lobley, C.M.,Soliman, F.,Kilkenny, M.L.,Smith, A.G.,Blundell, T.L.,Abell, C.
Structure of Escherichia coli aspartate alpha-decarboxylase Asn72Ala: probing the role of Asn72 in pyruvoyl cofactor formation
Acta Crystallogr.,Sect.F, 68:414-417, 2012

PubMed 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.

PubMed: 22505409
DOI: 10.1107/S1744309112009487

実験手法

X-RAY DIFFRACTION (1.7 Å)