1HQ6

STRUCTURE OF PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE AT PH 8

1HQ6 の概要

• エントリーDOI: 10.2210/pdb1hq6/pdb
• 関連するPDBエントリー: 1PYA
• 分子名称: HISTIDINE DECARBOXYLASE (3 entities in total)
• 機能のキーワード: helix disorder, ph regulation, less active form, pyruvoyl, carboxy-lyase, lyase
• 由来する生物種: Lactobacillus sp.; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 68272.41

構造登録者

Schelp, E.,Worley, S.,Monzingo, A.F.,Ernst, S.,Robertus, J.D. (登録日: 2000-12-14, 公開日: 2001-03-21, 最終更新日: 2024-11-20)

主引用文献

Schelp, E.,Worley, S.,Monzingo, A.F.,Ernst, S.,Robertus, J.D.
pH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a.
J.Mol.Biol., 306:727-732, 2001

PubMed Abstract: Histidine decarboxylase (HDC) from Lactobacillus 30a produces histamine that is essential to counter waste acids, and to optimize cell growth. The HDC trimer is active at low pH and inactive at neutral to alkaline pH. We have solved the X-ray structure of HDC at pH 8 and revealed the novel mechanism of pH regulation. At high pH helix B is unwound, destroying the substrate binding pocket. At acid pH the helix is stabilized, partly through protonation of Asp198 and Asp53 on either side of the molecular interface, acting as a proton trap. In contrast to hemoglobin regulation, pH has a large effect on the tertiary structure of HDC monomers and relatively little or no effect on quaternary structure.

PubMed: 11243783
DOI: 10.1006/jmbi.2000.4430

実験手法

X-RAY DIFFRACTION (2.7 Å)