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[[Image:1j12.gif|left|200px]]
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{{STRUCTURE_1j12|  PDB=1j12  |  SCENE=  }}
'''Beta-Amylase from Bacillus cereus var. mycoides in Complex with alpha-EBG'''


==Beta-Amylase from Bacillus cereus var. mycoides in Complex with alpha-EBG==
<StructureSection load='1j12' size='340' side='right'caption='[[1j12]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1j12]] 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=1J12 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J12 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]] 2.1&#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>, <scene name='pdbligand=EBG:2-HYDROXYMETHYL-6-(2-OXIRANYL-ETHOXY)-TETRAHYDRO-PYRAN-3,4,5-TRIOL'>EBG</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=1j12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j12 OCA], [https://pdbe.org/1j12 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j12 RCSB], [https://www.ebi.ac.uk/pdbsum/1j12 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j12 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/j1/1j12_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1j12 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structures of beta-amylase from Bacillus cereus var. mycoides in complexes with five inhibitors were solved. The inhibitors used were three substrate analogs, i.e. glucose, maltose (product), and a synthesized compound, O-alpha-D-glucopyranosyl-(1--&gt;4)-O-alpha-D-glucopyranosyl-(1--&gt;4)-D-xylopy ranose (GGX), and two affinity-labeling reagents with an epoxy alkyl group at the reducing end of glucose. For all inhibitors, one molecule was bound at the active site cleft and the non-reducing end glucose of the four inhibitors except GGX was located at subsite 1, accompanied by a large conformational change of the flexible loop (residues 93-97), which covered the bound inhibitor. In addition, another molecule of maltose or GGX was bound about 30 A away from the active site. A large movement of residues 330 and 331 around subsite 3 was also observed upon the binding of GGX at subsites 3 to 5. Two affinity-labeling reagents, alpha-EPG and alpha-EBG, were covalently bound to a catalytic residue (Glu-172). A substrate recognition mechanism for the beta-amylase was discussed based on the modes of binding of these inhibitors in the active site cleft.


==Overview==
Crystal structures of beta-amylase from Bacillus cereus var mycoides in complexes with substrate analogs and affinity-labeling reagents.,Oyama T, Miyake H, Kusunoki M, Nitta Y J Biochem. 2003 Apr;133(4):467-74. PMID:12761294<ref>PMID:12761294</ref>
The crystal structures of beta-amylase from Bacillus cereus var. mycoides in complexes with five inhibitors were solved. The inhibitors used were three substrate analogs, i.e. glucose, maltose (product), and a synthesized compound, O-alpha-D-glucopyranosyl-(1--&gt;4)-O-alpha-D-glucopyranosyl-(1--&gt;4)-D-xylopy ranose (GGX), and two affinity-labeling reagents with an epoxy alkyl group at the reducing end of glucose. For all inhibitors, one molecule was bound at the active site cleft and the non-reducing end glucose of the four inhibitors except GGX was located at subsite 1, accompanied by a large conformational change of the flexible loop (residues 93-97), which covered the bound inhibitor. In addition, another molecule of maltose or GGX was bound about 30 A away from the active site. A large movement of residues 330 and 331 around subsite 3 was also observed upon the binding of GGX at subsites 3 to 5. Two affinity-labeling reagents, alpha-EPG and alpha-EBG, were covalently bound to a catalytic residue (Glu-172). A substrate recognition mechanism for the beta-amylase was discussed based on the modes of binding of these inhibitors in the active site cleft.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1J12 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=1J12 OCA].
</div>
<div class="pdbe-citations 1j12" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structures of beta-amylase from Bacillus cereus var mycoides in complexes with substrate analogs and affinity-labeling reagents., Oyama T, Miyake H, Kusunoki M, Nitta Y, J Biochem. 2003 Apr;133(4):467-74. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12761294 12761294]
*[[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: Kusunoki M]]
[[Category: Kusunoki, M.]]
[[Category: Miyake H]]
[[Category: Miyake, H.]]
[[Category: Nitta Y]]
[[Category: Nitta, Y.]]
[[Category: Oyama T]]
[[Category: Oyama, T.]]
[[Category: Beta-amylase]]
[[Category: Hydrolase]]
[[Category: Raw-starch binding domain]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:40:22 2008''

Latest revision as of 09:37, 25 December 2024

Beta-Amylase from Bacillus cereus var. mycoides in Complex with alpha-EBG

1j12, resolution 2.10Å

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