5bca: Difference between revisions

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[[Image:5bca.png|left|200px]]
==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 [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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BCA FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5bca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bca OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5bca RCSB], [http://www.ebi.ac.uk/pdbsum/5bca PDBsum]</span></td></tr>
</table>
== 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/chain_selection.php?pdb_ID=2ata 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.


{{STRUCTURE_5bca|  PDB=5bca  |  SCENE=  }}
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>


===BETA-AMYLASE FROM BACILLUS CEREUS VAR. MYCOIDES===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_10348915}}
 
==About this Structure==
[[5bca]] is a 4 chain structure with 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].


==See Also==
==See Also==
*[[Alpha-Amylase|Alpha-Amylase]]
*[[Amylase|Amylase]]
 
*[[User:Gabriel Pons/Sandbox 2|User:Gabriel Pons/Sandbox 2]]
==Reference==
== References ==
<ref group="xtra">PMID:010348915</ref><references group="xtra"/>
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus cereus]]
[[Category: Bacillus cereus]]
[[Category: Beta-amylase]]
[[Category: Beta-amylase]]
[[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: Hydrolase]]
[[Category: Raw-starch binding domain]]
[[Category: Raw-starch binding domain]]