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| <StructureSection load='1e3x' size='340' side='right'caption='[[1e3x]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='1e3x' size='340' side='right'caption='[[1e3x]], [[Resolution|resolution]] 1.90Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1e3x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_amyloliquifaciens"_(sic)_fukumoto_1943 "bacillus amyloliquifaciens" (sic) fukumoto 1943]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E3X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E3X FirstGlance]. <br> | | <table><tr><td colspan='2'>[[1e3x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E3X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E3X FirstGlance]. <br> |
| </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=NA:SODIUM+ION'>NA</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]] 1.9Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1vjs|1vjs]], [[1bpl|1bpl]], [[1bli|1bli]], [[1e3z|1e3z]], [[1e40|1e40]], [[1e43|1e43]]</div></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=NA:SODIUM+ION'>NA</scene></td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] </span></td></tr>
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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e3x OCA], [https://pdbe.org/1e3x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e3x RCSB], [https://www.ebi.ac.uk/pdbsum/1e3x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e3x 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=1e3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e3x OCA], [https://pdbe.org/1e3x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e3x RCSB], [https://www.ebi.ac.uk/pdbsum/1e3x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e3x ProSAT]</span></td></tr> |
| </table> | | </table> |
| | == Function == |
| | [https://www.uniprot.org/uniprot/AMY_BACAM AMY_BACAM] |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| </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=1e3x ConSurf]. | | </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=1e3x ConSurf]. |
| <div style="clear:both"></div> | | <div style="clear:both"></div> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Several chimeric alpha-amylases genes were constructed by an in vivo recombination technique from the Bacillus amyloliquefaciens and Bacillus licheniformis genes. One of the fusion amylases (hereafter BA2), consisting of residues 1-300 from B. amyloliquefaciens and 301-483 from B. licheniformis, has been extensively studied by X-ray crystallography at resolutions between 2.2 and 1.7 A. The 3-dimensional structure of the native enzyme was solved by multiple isomorphous replacement, and refined at a resolution of 1.7 A. It consists of 483 amino acids, organized similarly to the known B. lichiniformis alpha-amylase structure [Machius et al. (1995) J. Mol. Biol. 246, 545-559], but features 4 bound calcium ions. Two of these form part of a linear cluster of three ions, the central ion being attributed to sodium. This cluster lies at the junction of the A and B domains with one calcium of the cluster structurally equivalent to the major Ca(2+) binding site of fungal alpha-amylases. The third calcium ion is found at the interface of the A and C domains. BA2 contains a fourth calcium site, not observed in the B. licheniformis alpha-amylase structure. It is found on the C domain where it bridges the two beta-sheets. Three acid residues (Glu261, Asp328, and Asp231) form an active site similar to that seen in other amylases. In the presence of TRIS buffer, a single molecule of TRIS occupies the -1 subsite of the enzyme where it is coordinated by the three active-center carboxylates. Kinetic data reveal that BA2 displays properties intermediate to those of its parents. Data for crystals soaked in maltooligosaccharides reveal the presence of a maltotriose binding site on the N-terminal face of the (beta/alpha)(8) barrel of the molecule, not previously described for any alpha-amylase structure, the biological function of which is unclear. Data for a complex soaked with the tetrasaccharide inhibitor acarbose, at 1.9 A, reveal a decasaccharide moiety, spanning the -7 to +3 subsites of the enzyme. The unambiguous presence of three unsaturated rings in the (2)H(3) half-chair/(2)E envelope conformation, adjacent to three 6-deoxypyranose units, clearly demonstrates synthesis of this acarbose-derived decasaccharide by a two-step transglycosylation mechanism.
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| Structural analysis of a chimeric bacterial alpha-amylase. High-resolution analysis of native and ligand complexes.,Brzozowski AM, Lawson DM, Turkenburg JP, Bisgaard-Frantzen H, Svendsen A, Borchert TV, Dauter Z, Wilson KS, Davies GJ Biochemistry. 2000 Aug 8;39(31):9099-107. PMID:10924103<ref>PMID:10924103</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 1e3x" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Amylase 3D structures|Amylase 3D structures]] | | *[[Amylase 3D structures|Amylase 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Alpha-amylase]] | | [[Category: Bacillus amyloliquefaciens]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Bisgaard-Frantzen, H]] | | [[Category: Bisgaard-Frantzen H]] |
| [[Category: Borchert, T V]] | | [[Category: Borchert TV]] |
| [[Category: Brzozowski, A M]] | | [[Category: Brzozowski AM]] |
| [[Category: Dauter, Z]] | | [[Category: Dauter Z]] |
| [[Category: Davies, G J]] | | [[Category: Davies GJ]] |
| [[Category: Lawson, D M]] | | [[Category: Lawson DM]] |
| [[Category: Svendsen, A]] | | [[Category: Svendsen A]] |
| [[Category: Turkenburg, J P]] | | [[Category: Turkenburg JP]] |
| [[Category: Wilson, K S]] | | [[Category: Wilson KS]] |
| [[Category: Amylase]]
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| [[Category: Family 13]]
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| [[Category: Hydrolase]]
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