1UHD

Crystal structure of aspartate decarboxylase, pyruvoly group bound form

1UHD の概要

• エントリーDOI: 10.2210/pdb1uhd/pdb
• 関連するPDBエントリー: 1UHE
• 分子名称: Aspartate 1-decarboxylase beta chain, Aspartate 1-decarboxylase alpha chain (3 entities in total)
• 機能のキーワード: double-psi beta barrel, lyase
• 由来する生物種: Helicobacter pylori; 詳細
• 細胞内の位置: Cytoplasm (By similarity): P56065 P56065
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13337.36

構造登録者

Lee, B.I.,Kwon, A.-R.,Han, B.W.,Suh, S.W. (登録日: 2003-07-01, 公開日: 2004-07-13, 最終更新日: 2024-11-20)

主引用文献

Lee, B.I.,Suh, S.W.
Crystal structure of the schiff base intermediate prior to decarboxylation in the catalytic cycle of aspartate alpha-decarboxylase
J.Mol.Biol., 340:1-7, 2004

PubMed Abstract: l-Aspartate alpha-decarboxylase (ADC), encoded by the panD gene, catalyzes the conversion of l-aspartate into beta-alanine. In the microorganisms, beta-alanine is required for the synthesis of pantothenate (vitamin B(5)), which is the precursor of 4'-phosphopantetheine and coenzyme A. We have determined the crystal structure of Helicobacter pylori ADC, a tetrameric enzyme, in two forms: the apo structure at 2.0 A resolution and the isoasparagine complex structure at 1.55 A resolution. All subunits of the tetramer are self-processed at the Gly24-Ser25 linkage, producing the smaller beta chain (residues 1-24) and the larger alpha chain (residues 25-117). Each subunit contains nine beta-strands and three alpha-helices; it is folded into the double-psi beta-barrel structure. In the apo structure, the new amino terminus of the alpha chain, Ser25, is converted into a pyruvoyl group. In the isoasparagine complex structure, the substrate analog is covalently attached to the pyruvoyl group. This structure represents the enzyme-substrate Schiff base intermediate that was proposed to form prior to the decarboxylation step in the catalytic cycle of ADC. Thus our study provides direct structural evidence for the reaction mechanism of ADC.

PubMed: 15184017
DOI: 10.1016/j.jmb.2004.04.049

実験手法

X-RAY DIFFRACTION (2 Å)