1ava
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1AVA is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ | + | 1AVA is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1]]. Structure known Active Sites: ACA and ACB. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AVA OCA]]. |
==Reference== | ==Reference== | ||
Barley alpha-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9 A resolution., Vallee F, Kadziola A, Bourne Y, Juy M, Rodenburg KW, Svensson B, Haser R, Structure. 1998 May 15;6(5):649-59. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9634702 9634702] | Barley alpha-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9 A resolution., Vallee F, Kadziola A, Bourne Y, Juy M, Rodenburg KW, Svensson B, Haser R, Structure. 1998 May 15;6(5):649-59. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9634702 9634702] | ||
| + | [[Category: Alpha-amylase]] | ||
[[Category: Hordeum vulgare]] | [[Category: Hordeum vulgare]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: hydrolase inhibition]] | [[Category: hydrolase inhibition]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:42:33 2007'' |
Revision as of 08:37, 30 October 2007
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AMY2/BASI PROTEIN-PROTEIN COMPLEX FROM BARLEY SEED
Overview
BACKGROUND: 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. RESULTS: The crystal structure of, AMY2 in complex with BASI was determined and refined at 1.9 A ... [(full description)]
About this Structure
1AVA is a [Protein complex] structure of sequences from [Hordeum vulgare] with CA as [ligand]. Active as [Alpha-amylase], with EC number [3.2.1.1]. Structure known Active Sites: ACA and ACB. Full crystallographic information is available from [OCA].
Reference
Barley alpha-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9 A resolution., Vallee F, Kadziola A, Bourne Y, Juy M, Rodenburg KW, Svensson B, Haser R, Structure. 1998 May 15;6(5):649-59. PMID:9634702
Page seeded by OCA on Tue Oct 30 10:42:33 2007
