4W1Y

Crystal structure of Escherichia coli Tryptophanase in 'semi-holo' form

4W1Y の概要

• エントリーDOI: 10.2210/pdb4w1y/pdb
• 関連するPDBエントリー: 2OQX 4W4H
• 分子名称: Tryptophanase, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: tryptophanase, lyase
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm : P0A853 P0A853
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 105045.61

構造登録者

Goldgur, Y. (登録日: 2014-08-13, 公開日: 2014-12-17, 最終更新日: 2023-12-27)

主引用文献

Kogan, A.,Raznov, L.,Gdalevsky, G.Y.,Cohen-Luria, R.,Almog, O.,Parola, A.H.,Goldgur, Y.
Structures of Escherichia coli tryptophanase in holo and `semi-holo' forms.
Acta Crystallogr.,Sect.F, 71:286-290, 2015

PubMed Abstract: Two crystal forms of Escherichia coli tryptophanase (tryptophan indole-lyase, Trpase) were obtained under the same crystallization conditions. Both forms belonged to the same space group P43212 but had slightly different unit-cell parameters. The holo crystal form, with pyridoxal phosphate (PLP) bound to Lys270 of both polypeptide chains in the asymmetric unit, diffracted to 2.9 Å resolution. The second crystal form diffracted to 3.2 Å resolution. Of the two subunits in the asymmetric unit, one was found in the holo form, while the other appeared to be in the apo form in a wide-open conformation with two sulfate ions bound in the vicinity of the active site. The conformation of all holo subunits is the same in both crystal forms. The structures suggest that Trpase is flexible in the apo form. Its conformation partially closes upon binding of PLP. The closed conformation might correspond to the enzyme in its active state with both cofactor and substrate bound in a similar way as in tyrosine phenol-lyase.

PubMed: 25760702
DOI: 10.1107/S2053230X15000850

実験手法

X-RAY DIFFRACTION (3.2 Å)