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[[Image:5bca.gif|left|200px]]
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{{STRUCTURE_5bca|  PDB=5bca  |  SCENE=  }}
'''BETA-AMYLASE FROM BACILLUS CEREUS VAR. MYCOIDES'''


==BETA-AMYLASE FROM BACILLUS CEREUS VAR. MYCOIDES==
<StructureSection load='5bca' size='340' side='right'caption='[[5bca]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5bca]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BCA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BCA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=5bca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bca OCA], [https://pdbe.org/5bca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bca RCSB], [https://www.ebi.ac.uk/pdbsum/5bca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bca ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AMYB_BACCE AMYB_BACCE]
== 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/bc/5bca_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=5bca ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of beta-amylase from Bacillus cereus var. mycoides was determined by the multiple isomorphous replacement method. The structure was refined to a final R-factor of 0.186 for 102,807 independent reflections with F/sigma(F) &gt; or = 2.0 at 2.2 A resolution with root-mean-square deviations from ideality in bond lengths, and bond angles of 0.014 A and 3.00 degrees, respectively. The asymmetric unit comprises four molecules exhibiting a dimer-of-dimers structure. The enzyme, however, acts as a monomer in solution. The beta-amylase molecule folds into three domains; the first one is the N-terminal catalytic domain with a (beta/alpha)8 barrel, the second one is the excursion part from the first one, and the third one is the C-terminal domain with two almost anti-parallel beta-sheets. The active site cleft, including two putative catalytic residues (Glu172 and Glu367), is located on the carboxyl side of the central beta-sheet in the (beta/alpha)8 barrel, as in most amylases. The active site structure of the enzyme resembles that of soybean beta-amylase with slight differences. One calcium ion is bound per molecule far from the active site. The C-terminal domain has a fold similar to the raw starch binding domains of cyclodextrin glycosyltransferase and glucoamylase.


==Overview==
Crystal structure of beta-amylase from Bacillus cereus var. mycoides at 2.2 A resolution.,Oyama T, Kusunoki M, Kishimoto Y, Takasaki Y, Nitta Y J Biochem. 1999 Jun;125(6):1120-30. PMID:10348915<ref>PMID:10348915</ref>
The crystal structure of beta-amylase from Bacillus cereus var. mycoides was determined by the multiple isomorphous replacement method. The structure was refined to a final R-factor of 0.186 for 102,807 independent reflections with F/sigma(F) &gt; or = 2.0 at 2.2 A resolution with root-mean-square deviations from ideality in bond lengths, and bond angles of 0.014 A and 3.00 degrees, respectively. The asymmetric unit comprises four molecules exhibiting a dimer-of-dimers structure. The enzyme, however, acts as a monomer in solution. The beta-amylase molecule folds into three domains; the first one is the N-terminal catalytic domain with a (beta/alpha)8 barrel, the second one is the excursion part from the first one, and the third one is the C-terminal domain with two almost anti-parallel beta-sheets. The active site cleft, including two putative catalytic residues (Glu172 and Glu367), is located on the carboxyl side of the central beta-sheet in the (beta/alpha)8 barrel, as in most amylases. The active site structure of the enzyme resembles that of soybean beta-amylase with slight differences. One calcium ion is bound per molecule far from the active site. The C-terminal domain has a fold similar to the raw starch binding domains of cyclodextrin glycosyltransferase and glucoamylase.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
5BCA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BCA OCA].
</div>
<div class="pdbe-citations 5bca" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structure of beta-amylase from Bacillus cereus var. mycoides at 2.2 A resolution., Oyama T, Kusunoki M, Kishimoto Y, Takasaki Y, Nitta Y, J Biochem. 1999 Jun;125(6):1120-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10348915 10348915]
*[[Amylase 3D structures|Amylase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus cereus]]
[[Category: Bacillus cereus]]
[[Category: Beta-amylase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Kishimoto Y]]
[[Category: Kishimoto, Y.]]
[[Category: Kusunoki M]]
[[Category: Kusunoki, M.]]
[[Category: Nitta Y]]
[[Category: Nitta, Y.]]
[[Category: Oyama T]]
[[Category: Oyama, T.]]
[[Category: Takasaki Y]]
[[Category: Takasaki, Y.]]
[[Category: Beta-amylase]]
[[Category: Hydrolase]]
[[Category: Raw-starch binding domain]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:32:05 2008''
Retrieved from "https://proteopedia.org/5bca"