1bfn
From Proteopedia
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|PDB= 1bfn |SIZE=350|CAPTION= <scene name='initialview01'>1bfn</scene>, resolution 2.07Å | |PDB= 1bfn |SIZE=350|CAPTION= <scene name='initialview01'>1bfn</scene>, resolution 2.07Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Beta-amylase Beta-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.2 3.2.1.2] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-amylase Beta-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.2 3.2.1.2] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bfn OCA], [http://www.ebi.ac.uk/pdbsum/1bfn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bfn RCSB]</span> | ||
}} | }} | ||
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[[Category: Mikami, B.]] | [[Category: Mikami, B.]] | ||
[[Category: Utsumi, S.]] | [[Category: Utsumi, S.]] | ||
| - | [[Category: SO4]] | ||
[[Category: beta-amylase]] | [[Category: beta-amylase]] | ||
[[Category: beta-cyclodextrin]] | [[Category: beta-cyclodextrin]] | ||
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[[Category: recombinant]] | [[Category: recombinant]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:59:59 2008'' |
Revision as of 16:00, 30 March 2008
| |||||||
| , resolution 2.07Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Beta-amylase, with EC number 3.2.1.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BETA-AMYLASE/BETA-CYCLODEXTRIN COMPLEX
Overview
In order to study the interaction of soybean beta-amylase with substrate, we solved the crystal structure of beta-cyclodextrin-enzyme complex and compared it with that of alpha-cyclodextrin-enzyme complex. The enzyme was expressed in Escherichia coli at a high level as a soluble and catalytically active protein. The purified recombinant enzyme had properties nearly identical to those of native soybean beta-amylase and formed the same crystals as the native enzyme. The crystal structure of recombinant enzyme complexed with beta-cyclodextrin was refined at 2. 07-A resolution with a final crystallographic R value of 15.8% (Rfree = 21.1%). The root mean square deviation in the position of C-alpha atoms between this recombinant enzyme and the native enzyme was 0.22 A. These results indicate that the expression system established here is suitable for studying structure-function relationships of beta-amylase. The conformation of the bound beta-cyclodextrin takes an ellipsoid shape in contrast to the circular shape of the bound alpha-cyclodextrin. The cyclodextrins shared mainly two glucose binding sites, 3 and 4. The glucose residue 4 was slightly shifted from the maltose binding site. This suggests that the binding site of the cyclodextrins is important for its holding of a cleaved substrate, which enables the multiple attack mechanism of beta-amylase.
About this Structure
1BFN is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.
Reference
Crystal structure of recombinant soybean beta-amylase complexed with beta-cyclodextrin., Adachi M, Mikami B, Katsube T, Utsumi S, J Biol Chem. 1998 Jul 31;273(31):19859-65. PMID:9677422
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