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2DQA

Crystal Structure of Tapes japonica Lysozyme

2DQA の概要
エントリーDOI10.2210/pdb2dqa/pdb
関連するBIRD辞書のPRD_IDPRD_900017
分子名称Lysozyme, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, PLATINUM (II) ION, ... (5 entities in total)
機能のキーワードlysozyme, enzyme, substrate complex, hydrolase
由来する生物種Tapes japonica
タンパク質・核酸の鎖数2
化学式量合計30938.59
構造登録者
Goto, T.,Kakuta, Y.,Abe, Y.,Takeshita, K.,Imoto, T.,Ueda, T. (登録日: 2006-05-24, 公開日: 2007-06-12, 最終更新日: 2024-10-16)
主引用文献Goto, T.,Abe, Y.,Kakuta, Y.,Takeshita, K.,Imoto, T.,Ueda, T.
Crystal Structure of Tapes japonica Lysozyme with Substrate Analogue: STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND MANIFESTATION OF ITS CHITINASE ACTIVITY ACCOMPANIED BY QUATERNARY STRUCTURAL CHANGE
J.Biol.Chem., 282:27459-27467, 2007
Cited by
PubMed Abstract: Tapes japonica lysozyme (TJL) is classified as a member of the recently established i-type lysozyme family. In this study, we solved the crystal structure of TJL complexed with a trimer of N-acetylglucosamine to 1.6A resolution. Based on structure and mutation analyses, we demonstrated that Glu-18 and Asp-30 are the catalytic residues of TJL. Furthermore, the present findings suggest that the catalytic mechanism of TJL is a retaining mechanism that proceeds through a covalent sugar-enzyme intermediate. On the other hand, the quaternary structure in the crystal revealed a dimer formed by the electrostatic interactions of catalytic residues (Glu-18 and Asp-30) in one molecule with the positive residues at the C terminus in helix 6 of the other molecule. Gel chromatography analysis revealed that the TJL dimer remained intact under low salt conditions but that it dissociated to TJL monomers under high salt conditions. With increasing salt concentrations, the chitinase activity of TJL dramatically increased. Therefore, this study provides novel evidence that the lysozyme activity of TJL is modulated by its quaternary structure.
PubMed: 17631496
DOI: 10.1074/jbc.M704555200
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.6 Å)
構造検証レポート
Validation report summary of 2dqa
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-21に公開中

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