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| | ==Barley alpha-amylase isozyme 1 (AMY1) H395A mutant== | | ==Barley alpha-amylase isozyme 1 (AMY1) H395A mutant== |
| - | <StructureSection load='3bsg' size='340' side='right' caption='[[3bsg]], [[Resolution|resolution]] 1.95Å' scene=''> | + | <StructureSection load='3bsg' size='340' side='right'caption='[[3bsg]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3bsg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Barley Barley]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BSG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BSG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3bsg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BSG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BSG 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]] 1.95Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ht6|1ht6]], [[3bsh|3bsh]]</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='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=3bsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bsg OCA], [https://pdbe.org/3bsg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bsg RCSB], [https://www.ebi.ac.uk/pdbsum/3bsg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bsg ProSAT]</span></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=3bsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bsg OCA], [http://pdbe.org/3bsg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bsg RCSB], [http://www.ebi.ac.uk/pdbsum/3bsg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bsg ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/AMY1_HORVU AMY1_HORVU] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Amylase|Amylase]] | + | *[[Amylase 3D structures|Amylase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alpha-amylase]] | + | [[Category: Hordeum vulgare]] |
| - | [[Category: Barley]] | + | [[Category: Large Structures]] |
| - | [[Category: Aghajari, N]] | + | [[Category: Aghajari N]] |
| - | [[Category: Haser, R]] | + | [[Category: Haser R]] |
| - | [[Category: Robert, X]] | + | [[Category: Robert X]] |
| - | [[Category: Amy1]]
| + | |
| - | [[Category: Barley alpha-amylase]]
| + | |
| - | [[Category: Calcium]]
| + | |
| - | [[Category: Carbohydrate metabolism]]
| + | |
| - | [[Category: Germination]]
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| - | [[Category: Glycosidase]]
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| - | [[Category: Hydrolase]]
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| - | [[Category: Metal-binding]]
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| - | [[Category: Mutant]]
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| - | [[Category: Secreted]]
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| Structural highlights
Function
AMY1_HORVU
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
Certain starch hydrolases possess secondary carbohydrate binding sites outside of the active site, suggesting that multi-site substrate interactions are functionally significant. In barley alpha-amylase both Tyr380, situated on a remote non-catalytic domain, and Tyr105 in subsite -6 of the active site cleft are principal carbohydrate binding residues. The dual active site/secondary site mutants Y105A/Y380A and Y105A/Y380M show that each of Tyr380 and Tyr105 is important, albeit not essential for binding, degradation, and multiple attack on polysaccharides, while Tyr105 predominates in oligosaccharide hydrolysis. Additional delicate structure/function relationships of the secondary site are uncovered using Y380A/H395A, Y380A, and H395A AMY1 mutants.
Multi-site substrate binding and interplay in barley alpha-amylase 1.,Nielsen MM, Seo ES, Bozonnet S, Aghajari N, Robert X, Haser R, Svensson B FEBS Lett. 2008 Jul 23;582(17):2567-71. Epub 2008 Jun 25. PMID:18588886[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nielsen MM, Seo ES, Bozonnet S, Aghajari N, Robert X, Haser R, Svensson B. Multi-site substrate binding and interplay in barley alpha-amylase 1. FEBS Lett. 2008 Jul 23;582(17):2567-71. Epub 2008 Jun 25. PMID:18588886 doi:10.1016/j.febslet.2008.06.027
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