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3bsg

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{{Seed}}
 
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[[Image:3bsg.png|left|200px]]
 
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<!--
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==Barley alpha-amylase isozyme 1 (AMY1) H395A mutant==
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The line below this paragraph, containing "STRUCTURE_3bsg", creates the "Structure Box" on the page.
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<StructureSection load='3bsg' size='340' side='right'caption='[[3bsg]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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<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>
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{{STRUCTURE_3bsg| PDB=3bsg | SCENE= }}
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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=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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AMY1_HORVU AMY1_HORVU]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bs/3bsg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=3bsg ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Barley alpha-amylase isozyme 1 (AMY1) H395A mutant===
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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<ref>PMID:18588886</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3bsg" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18588886}}, adds the Publication Abstract to the page
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*[[Amylase 3D structures|Amylase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18588886 is the PubMed ID number.
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== References ==
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-->
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<references/>
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{{ABSTRACT_PUBMED_18588886}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3BSG is a 1 chain structure of sequence from [http://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].
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==Reference==
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<ref group="xtra">PMID:18588886</ref><references group="xtra"/>
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[[Category: Alpha-amylase]]
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[[Category: Hordeum vulgare]]
[[Category: Hordeum vulgare]]
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[[Category: Aghajari, N.]]
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[[Category: Large Structures]]
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[[Category: Haser, R.]]
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[[Category: Aghajari N]]
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[[Category: Robert, X.]]
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[[Category: Haser R]]
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[[Category: Amy1]]
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[[Category: Robert X]]
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[[Category: Barley alpha-amylase]]
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[[Category: Calcium]]
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[[Category: Carbohydrate metabolism]]
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[[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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 07:45:38 2009''
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Current revision

Barley alpha-amylase isozyme 1 (AMY1) H395A mutant

PDB ID 3bsg

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