3bsh: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:3bsh.png|left|200px]]
-<!--
+==Barley alpha-amylase isozyme 1 (AMY1) double mutant Y105A/Y380A in complex with inhibitor acarbose==
-The line below this paragraph, containing "STRUCTURE_3bsh", creates the "Structure Box" on the page.
+<StructureSection load='3bsh' size='340' side='right'caption='[[3bsh]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3bsh]] 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=3BSH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BSH FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-{{STRUCTURE_3bsh|  PDB=3bsh  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bsh OCA], [https://pdbe.org/3bsh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bsh RCSB], [https://www.ebi.ac.uk/pdbsum/3bsh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bsh ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/AMY1_HORVU AMY1_HORVU]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <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>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=3bsh ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-===Barley alpha-amylase isozyme 1 (AMY1) double mutant Y105A/Y380A in complex with inhibitor acarbose===
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3bsh" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_18588886}}, adds the Publication Abstract to the page
+*[[Amylase 3D structures|Amylase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 18588886 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_18588886}}
+__TOC__
+</StructureSection>
-==About this Structure==
-BSH 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=3BSH OCA].
-==Reference==
-<ref group="xtra">PMID:18588886</ref><references group="xtra"/>
-[[Category: Alpha-amylase]]
 [[Category: Hordeum vulgare]]
-[[Category: Aghajari, N.]]
+[[Category: Large Structures]]
-[[Category: Haser, R.]]
+[[Category: Aghajari N]]
-[[Category: Robert, X.]]
+[[Category: Haser R]]
-[[Category: Acarbose]]
+[[Category: Robert X]]
-[[Category: Amy1]]
-[[Category: Barley alpha-amylase]]
-[[Category: Calcium]]
-[[Category: Carbohydrate metabolism]]
-[[Category: Complex]]
-[[Category: Germination]]
-[[Category: Glycosidase]]
-[[Category: Hydrolase]]
-[[Category: Metal-binding]]
-[[Category: Mutant]]
-[[Category: Secreted]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 04:00:25 2009''