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[[Image:1bfn.gif|left|200px]]


{{Structure
==BETA-AMYLASE/BETA-CYCLODEXTRIN COMPLEX==
|PDB= 1bfn |SIZE=350|CAPTION= <scene name='initialview01'>1bfn</scene>, resolution 2.07&Aring;
<StructureSection load='1bfn' size='340' side='right'caption='[[1bfn]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
<table><tr><td colspan='2'>[[1bfn]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BFN FirstGlance]. <br>
|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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.07&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900012:beta-cyclodextrin'>PRD_900012</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bfn OCA], [https://pdbe.org/1bfn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bfn RCSB], [https://www.ebi.ac.uk/pdbsum/1bfn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bfn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AMYB_SOYBN AMYB_SOYBN]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/1bfn_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bfn ConSurf].
<div style="clear:both"></div>


'''BETA-AMYLASE/BETA-CYCLODEXTRIN COMPLEX'''
==See Also==
 
*[[Amylase 3D structures|Amylase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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 [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==
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: Glycine max]]
[[Category: Glycine max]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Adachi, M.]]
[[Category: Adachi M]]
[[Category: Katsube, T.]]
[[Category: Katsube T]]
[[Category: Mikami, B.]]
[[Category: Mikami B]]
[[Category: Utsumi, S.]]
[[Category: Utsumi S]]
[[Category: SO4]]
[[Category: beta-amylase]]
[[Category: beta-cyclodextrin]]
[[Category: hydrolase]]
[[Category: recombinant]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:10:22 2008''

Latest revision as of 06:35, 7 February 2024

BETA-AMYLASE/BETA-CYCLODEXTRIN COMPLEX

1bfn, resolution 2.07Å

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