4UP2

Crystal structure of Escherichia coli tryptophanase purified from alkaline stressed bacterial culture.

4UP2 の概要

• エントリーDOI: 10.2210/pdb4up2/pdb
• 関連するPDBエントリー: 4UP1
• 分子名称: TRYPTOPHANASE, SULFATE ION, BETA-MERCAPTOETHANOL, ... (4 entities in total)
• 機能のキーワード: lyase, alkaline stress, protein purification
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 214168.96

構造登録者

Rety, S.,Deschamps, P.,Leulliot, N. (登録日: 2014-06-11, 公開日: 2015-06-24, 最終更新日: 2024-01-10)

主引用文献

Rety, S.,Deschamps, P.,Leulliot, N.
Structure of Escherichia Coli Tryptophanase Purified from an Alkaline-Stressed Bacterial Culture.
Acta Crystallogr.,Sect.F, 71:1378-, 2015

PubMed Abstract: Tryptophanase is a bacterial enzyme involved in the degradation of tryptophan to indole, pyruvate and ammonia, which are compounds that are essential for bacterial survival. Tryptophanase is often overexpressed in stressed cultures. Large amounts of endogenous tryptophanase were purified from Escherichia coli BL21 strain overexpressing another recombinant protein. Tryptophanase was crystallized in space group P6522 in the apo form without pyridoxal 5'-phosphate bound in the active site.

PubMed: 26527264
DOI: 10.1107/S2053230X15017549

実験手法

X-RAY DIFFRACTION (2.78 Å)