1AVA

AMY2/BASI PROTEIN-PROTEIN COMPLEX FROM BARLEY SEED

1AVA の概要

• エントリーDOI: 10.2210/pdb1ava/pdb
• 分子名称: BARLEY ALPHA-AMYLASE 2(CV MENUET), BARLEY ALPHA-AMYLASE/SUBTILISIN INHIBITOR, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: hydrolase inhibition, enzyme inhibitor complex
• 由来する生物種: Hordeum vulgare; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 130110.13

構造登録者

Vallee, F.,Kadziola, A.,Bourne, Y.,Juy, M.,Svensson, B.,Haser, R. (登録日: 1997-09-15, 公開日: 1999-03-16, 最終更新日: 2024-10-23)

主引用文献

Vallee, F.,Kadziola, A.,Bourne, Y.,Juy, M.,Rodenburg, K.W.,Svensson, B.,Haser, R.
Barley alpha-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9 A resolution.
Structure, 6:649-659, 1998

PubMed Abstract: Barley alpha-amylase is a 45 kDa enzyme which is involved in starch degradation during barley seed germination. The released sugars provide the plant embryo with energy for growth. The major barley alpha-amylase isozyme (AMY2) binds with high affinity to the endogenous inhibitor BASI (barley alpha-amylase/subtilisin inhibitor) whereas the minor isozyme (AMY1) is not inhibited. BASI is a 19.6 kDa bifunctional protein that can simultaneously inhibit AMY2 and serine proteases of the subtilisin family. This inhibitor may therefore prevent degradation of the endosperm starch during premature sprouting and protect the seed from attack by pathogens secreting proteases.

PubMed: 9634702
DOI: 10.1016/S0969-2126(98)00066-5

実験手法

X-RAY DIFFRACTION (1.9 Å)