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1bfn

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[[Image:1bfn.gif|left|200px]]
[[Image:1bfn.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1bfn |SIZE=350|CAPTION= <scene name='initialview01'>1bfn</scene>, resolution 2.07&Aring;
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The line below this paragraph, containing "STRUCTURE_1bfn", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1bfn| PDB=1bfn | SCENE= }}
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|RELATEDENTRY=
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|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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}}
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'''BETA-AMYLASE/BETA-CYCLODEXTRIN COMPLEX'''
'''BETA-AMYLASE/BETA-CYCLODEXTRIN COMPLEX'''
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[[Category: Mikami, B.]]
[[Category: Mikami, B.]]
[[Category: Utsumi, S.]]
[[Category: Utsumi, S.]]
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[[Category: beta-amylase]]
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[[Category: Beta-amylase]]
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[[Category: beta-cyclodextrin]]
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[[Category: Beta-cyclodextrin]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: recombinant]]
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[[Category: Recombinant]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:27:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:59:59 2008''
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Revision as of 08:27, 2 May 2008

Template:STRUCTURE 1bfn

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 Page seeded by OCA on Fri May 2 11:27:01 2008

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