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[[Image:1b90.gif|left|200px]]
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{{STRUCTURE_1b90|  PDB=1b90  |  SCENE=  }}
'''BACILLUS CEREUS BETA-AMYLASE APO FORM'''


==BACILLUS CEREUS BETA-AMYLASE APO FORM==
<StructureSection load='1b90' size='340' side='right'caption='[[1b90]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1b90]] is a 1 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=1B90 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B90 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1b90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b90 OCA], [https://pdbe.org/1b90 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b90 RCSB], [https://www.ebi.ac.uk/pdbsum/1b90 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b90 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/b9/1b90_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=1b90 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystals of beta-amylase from Bacillus cereus belong to space group P21 with the following cell dimensions: a = 57.70 A, b = 92.87 A, c = 65.93 A, and beta =101.95 degrees. The structures of free and maltose-bound beta-amylases were determined by X-ray crystallography at 2.1 and 2.5 A with R-factors of 0.170 and 0.164, respectively. The final model of the maltose-bound form comprises 516 amino acid residues, four maltose molecules, 275 water molecules, one Ca2+, one acetate, and one sulfate ion. The enzyme consists of a core (beta/alpha)8-barrel domain (residues 5-434) and a C-terminal starch-binding domain (residues 435-613). Besides the active site in the core where two maltose molecules are bound in tandem, two novel maltose-binding sites were found in the core L4 region and in the C-terminal domain. The structure of the core domain is similar to that of soybean beta-amylase except for the L4 maltose-binding site, whereas the C-terminal domain has the same secondary structure as domain E of cyclodextrin glucosyltransferase. These two maltose-binding sites are 32-36 A apart from the active site. These results indicate that the ability of B. cereus beta-amylase to digest raw starch can be attributed to the additional two maltose-binding sites.


==Overview==
Structure of raw starch-digesting Bacillus cereus beta-amylase complexed with maltose.,Mikami B, Adachi M, Kage T, Sarikaya E, Nanmori T, Shinke R, Utsumi S Biochemistry. 1999 Jun 1;38(22):7050-61. PMID:10353816<ref>PMID:10353816</ref>
The crystals of beta-amylase from Bacillus cereus belong to space group P21 with the following cell dimensions: a = 57.70 A, b = 92.87 A, c = 65.93 A, and beta =101.95 degrees. The structures of free and maltose-bound beta-amylases were determined by X-ray crystallography at 2.1 and 2.5 A with R-factors of 0.170 and 0.164, respectively. The final model of the maltose-bound form comprises 516 amino acid residues, four maltose molecules, 275 water molecules, one Ca2+, one acetate, and one sulfate ion. The enzyme consists of a core (beta/alpha)8-barrel domain (residues 5-434) and a C-terminal starch-binding domain (residues 435-613). Besides the active site in the core where two maltose molecules are bound in tandem, two novel maltose-binding sites were found in the core L4 region and in the C-terminal domain. The structure of the core domain is similar to that of soybean beta-amylase except for the L4 maltose-binding site, whereas the C-terminal domain has the same secondary structure as domain E of cyclodextrin glucosyltransferase. These two maltose-binding sites are 32-36 A apart from the active site. These results indicate that the ability of B. cereus beta-amylase to digest raw starch can be attributed to the additional two maltose-binding sites.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1B90 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=1B90 OCA].
</div>
<div class="pdbe-citations 1b90" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structure of raw starch-digesting Bacillus cereus beta-amylase complexed with maltose., Mikami B, Adachi M, Kage T, Sarikaya E, Nanmori T, Shinke R, Utsumi S, Biochemistry. 1999 Jun 1;38(22):7050-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10353816 10353816]
*[[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: Adachi M]]
[[Category: Adachi, M.]]
[[Category: Kage T]]
[[Category: Kage, T.]]
[[Category: Mikami B]]
[[Category: Mikami, B.]]
[[Category: Nanmori T]]
[[Category: Nanmori, T.]]
[[Category: Sarikaya E]]
[[Category: Sarikaya, E.]]
[[Category: Shinke R]]
[[Category: Shinke, R.]]
[[Category: Utsumi S]]
[[Category: Utsumi, S.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:13:32 2008''
Retrieved from "https://proteopedia.org/1b90"