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| | <StructureSection load='6tp2' size='340' side='right'caption='[[6tp2]], [[Resolution|resolution]] 1.94Å' scene=''> | | <StructureSection load='6tp2' size='340' side='right'caption='[[6tp2]], [[Resolution|resolution]] 1.94Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6tp2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"clostridium_licheniforme"_weigmann_1898 "clostridium licheniforme" weigmann 1898]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TP2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TP2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6tp2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TP2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TP2 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=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</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]] 1.94Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">amy ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1402 "Clostridium licheniforme" Weigmann 1898])</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=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PRD_900012:beta-cyclodextrin'>PRD_900012</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] </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=6tp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tp2 OCA], [https://pdbe.org/6tp2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tp2 RCSB], [https://www.ebi.ac.uk/pdbsum/6tp2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tp2 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6tp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tp2 OCA], [http://pdbe.org/6tp2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tp2 RCSB], [http://www.ebi.ac.uk/pdbsum/6tp2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tp2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/I3P686_BACLI I3P686_BACLI] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6tp2" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6tp2" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Amylase 3D structures|Amylase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Clostridium licheniforme weigmann 1898]] | + | [[Category: Bacillus licheniformis]] |
| - | [[Category: Alpha-amylase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Janssen, D B]] | + | [[Category: Janssen DB]] |
| - | [[Category: Rozeboom, H J]] | + | [[Category: Rozeboom HJ]] |
| - | [[Category: Amylase]]
| + | |
| - | [[Category: Cyclodextrin]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Starch binding site]]
| + | |
| Structural highlights
6tp2 is a 1 chain structure with sequence from Bacillus licheniformis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.94Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
I3P686_BACLI
Publication Abstract from PubMed
alpha-Amylase from Bacillus paralicheniformis (BliAmy), belonging to GH13_5 subfamily of glycoside hydrolases, was proven to be a highly efficient raw starch digesting enzyme. The ability of some alpha-amylases to hydrolyze raw starch is related to the existence of surface binding sites (SBSs) for polysaccharides that can be distant from the active site. Crystallographic studies performed on BliAmy in the apo form and of enzyme bound with different oligosaccharides and oligosaccharide precursors revealed binding of these ligands to one SBS with two amino acids F257 and Y358 mainly involved in complex formation. The role of this SBS in starch binding and degradation was probed by designing enzyme variants mutated in this region (F257A and Y358A). Kinetic studies with different substrates show that starch binding through the SBS is disrupted in the mutants and that F257 and Y358 contributed cumulatively to binding and hydrolysis. Mutation of both sites (F257A/Y358A) resulted in a 5-fold lower efficacy with raw starch as substrate and at least 5.5-fold weaker binding compared to the wild type BliAmy, suggesting that the ability of BliAmy to hydrolyze raw starch with high efficiency is related to the level of its adsorption onto starch granules.
Characterization of the starch surface binding site on Bacillus paralicheniformis alpha-amylase.,Bozic N, Rozeboom HJ, Loncar N, Slavic MS, Janssen DB, Vujcic Z Int J Biol Macromol. 2020 Oct 12. pii: S0141-8130(20)34647-X. doi:, 10.1016/j.ijbiomac.2020.10.025. PMID:33058974[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bozic N, Rozeboom HJ, Loncar N, Slavic MS, Janssen DB, Vujcic Z. Characterization of the starch surface binding site on Bacillus paralicheniformis alpha-amylase. Int J Biol Macromol. 2020 Oct 12. pii: S0141-8130(20)34647-X. doi:, 10.1016/j.ijbiomac.2020.10.025. PMID:33058974 doi:http://dx.doi.org/10.1016/j.ijbiomac.2020.10.025
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