2V1P

Crystal Structure of the apo form of Y74F mutant E. coli tryptophanase

2V1P の概要

• エントリーDOI: 10.2210/pdb2v1p/pdb
• 関連するPDBエントリー: 2C44 2V0Y
• 分子名称: TRYPTHOPANASE, CHLORIDE ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: lyase, pyridoxal phosphate, tryptophan catabolism
• 由来する生物種: ESCHERICHIA COLI
• 細胞内の位置: Cytoplasm : P0A853
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52508.68

構造登録者

Kogan, A.,Gdalevsky, G.Y.,Cohen-Luria, R.,Goldgur, Y.,Parola, A.H.,Almog, O. (登録日: 2007-05-28, 公開日: 2008-06-10, 最終更新日: 2024-11-20)

主引用文献

Kogan, A.,Gdalevsky, G.Y.,Cohen-Luria, R.,Goldgur, Y.,Phillips, R.S.,Parola, A.H.,Almog, O.
Conformational Changes and Loose Packing Promote E. Coli Tryptophanase Cold Lability.
Bmc Struct.Biol., 9:65-, 2009

PubMed Abstract: Oligomeric enzymes can undergo a reversible loss of activity at low temperatures. One such enzyme is tryptophanase (Trpase) from Escherichia coli. Trpase is a pyridoxal phosphate (PLP)-dependent tetrameric enzyme with a Mw of 210 kD. PLP is covalently bound through an enamine bond to Lys270 at the active site. The incubation of holo E. coli Trpases at 2 degrees C for 20 h results in breaking this enamine bond and PLP release, as well as a reversible loss of activity and dissociation into dimers. This sequence of events is termed cold lability and its understanding bears relevance to protein stability and shelf life.

PubMed: 19814824
DOI: 10.1186/1472-6807-9-65

実験手法

X-RAY DIFFRACTION (1.9 Å)