3bsh: Difference between revisions
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==Barley alpha-amylase isozyme 1 (AMY1) double mutant Y105A/Y380A in complex with inhibitor acarbose== | ==Barley alpha-amylase isozyme 1 (AMY1) double mutant Y105A/Y380A in complex with inhibitor acarbose== | ||
<StructureSection load='3bsh' size='340' side='right' caption='[[3bsh]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='3bsh' size='340' side='right' caption='[[3bsh]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ht6|1ht6]], [[3bsg|3bsg]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ht6|1ht6]], [[3bsg|3bsg]]</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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bsh OCA], [http://pdbe.org/3bsh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bsh RCSB], [http://www.ebi.ac.uk/pdbsum/3bsh PDBsum]</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=3bsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bsh OCA], [http://pdbe.org/3bsh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bsh RCSB], [http://www.ebi.ac.uk/pdbsum/3bsh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bsh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bs/3bsh_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bs/3bsh_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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==See Also== | ==See Also== | ||
*[[Amylase|Amylase]] | *[[Amylase|Amylase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Amy1]] | [[Category: Amy1]] | ||
[[Category: Barley alpha-amylase]] | [[Category: Barley alpha-amylase]] | ||
[[Category: Calcium]] | |||
[[Category: Carbohydrate metabolism]] | [[Category: Carbohydrate metabolism]] | ||
[[Category: Complex]] | [[Category: Complex]] | ||
Revision as of 11:15, 31 October 2018
Barley alpha-amylase isozyme 1 (AMY1) double mutant Y105A/Y380A in complex with inhibitor acarboseBarley alpha-amylase isozyme 1 (AMY1) double mutant Y105A/Y380A in complex with inhibitor acarbose
Structural highlights
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 PubMedCertain 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 AlsoReferences
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