1ECY

PROTEASE INHIBITOR ECOTIN

1ECY の概要

• エントリーDOI: 10.2210/pdb1ecy/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900006
• 分子名称: ECOTIN, alpha-D-glucopyranose-(1-1)-alpha-D-glucopyranose, alpha-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: beta-sheet structure, serine protease inhibitor, periplasmic, protease inhibitor
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21471.15

構造登録者

Shin, D.H.,Suh, S.W. (登録日: 1996-08-06, 公開日: 1997-02-12, 最終更新日: 2024-10-30)

主引用文献

Shin, D.H.,Song, H.K.,Seong, I.S.,Lee, C.S.,Chung, C.H.,Suh, S.W.
Crystal structure analyses of uncomplexed ecotin in two crystal forms: implications for its function and stability.
Protein Sci., 5:2236-2247, 1996

PubMed Abstract: Ecotin, a homodimeric protein composed of 142 residue subunits, is a novel serine protease inhibitor present in Escherichia coli. Its thermostability and acid stability, as well as broad specificity toward proteases, make it an interesting protein for structural characterization. Its structure in the uncomplexed state, determined for two different crystalline environments, allows a structural comparison of the free inhibitor with that in complex with trypsin. Although there is no gross structural rearrangement of ecotin when binding trypsin, the loops involved in binding trypsin show relatively large shifts in atomic positions. The inherent flexibility of the loops and the highly nonglobular shape are the two features essential for its inhibitory function. An insight into the understanding of the structural basis of thermostability and acid stability of ecotin is also provided by the present structure.

PubMed: 8931142

実験手法

X-RAY DIFFRACTION (2.19 Å)