1bfn: Difference between revisions
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[[Image:1bfn.gif|left|200px]] | [[Image:1bfn.gif|left|200px]] | ||
'''BETA-AMYLASE/BETA-CYCLODEXTRIN COMPLEX''' | {{Structure | ||
|PDB= 1bfn |SIZE=350|CAPTION= <scene name='initialview01'>1bfn</scene>, resolution 2.07Å | |||
|SITE= | |||
|LIGAND= <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] | |||
|GENE= | |||
}} | |||
'''BETA-AMYLASE/BETA-CYCLODEXTRIN COMPLEX''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1BFN is a [ | 1BFN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BFN OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9677422 9677422] | ||
[[Category: Beta-amylase]] | [[Category: Beta-amylase]] | ||
[[Category: Glycine max]] | [[Category: Glycine max]] | ||
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[[Category: recombinant]] | [[Category: recombinant]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:10:22 2008'' | ||
Revision as of 08:10, 20 March 2008
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| 1bfn, resolution 2.07Å | |||||||||||||
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| Ligands: | SO4 | ||||||||||||
| Activity: | Beta-amylase, with EC number 3.2.1.2 | ||||||||||||
| 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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