1AVA

AMY2/BASI PROTEIN-PROTEIN COMPLEX FROM BARLEY SEED

Summary for 1AVA

• Entry DOI: 10.2210/pdb1ava/pdb
• Descriptor: BARLEY ALPHA-AMYLASE 2(CV MENUET), BARLEY ALPHA-AMYLASE/SUBTILISIN INHIBITOR, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: hydrolase inhibition, enzyme inhibitor complex
• Biological source: Hordeum vulgare; More
• Total number of polymer chains: 4
• Total formula weight: 130110.13

Authors

Vallee, F.,Kadziola, A.,Bourne, Y.,Juy, M.,Svensson, B.,Haser, R. (deposition date: 1997-09-15, release date: 1999-03-16, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)