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| | <StructureSection load='5bca' size='340' side='right'caption='[[5bca]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='5bca' size='340' side='right'caption='[[5bca]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == 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> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</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='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'>[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://pdbe.org/5bca PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bca RCSB], [http://www.ebi.ac.uk/pdbsum/5bca PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bca ProSAT]</span></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> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/AMYB_BACCE AMYB_BACCE] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Bacillus cereus]] | | [[Category: Bacillus cereus]] |
| - | [[Category: Beta-amylase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[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: Hydrolase]]
| + | |
| - | [[Category: Raw-starch binding domain]]
| + | |
| Structural highlights
Function
AMYB_BACCE
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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) > 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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Oyama T, Kusunoki M, Kishimoto Y, Takasaki Y, Nitta Y. Crystal structure of beta-amylase from Bacillus cereus var. mycoides at 2.2 A resolution. J Biochem. 1999 Jun;125(6):1120-30. PMID:10348915
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