1jf6: Difference between revisions
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==Crystal structure of thermoactinomyces vulgaris r-47 alpha-amylase mutant F286Y== | ==Crystal structure of thermoactinomyces vulgaris r-47 alpha-amylase mutant F286Y== | ||
<StructureSection load='1jf6' size='340' side='right' caption='[[1jf6]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='1jf6' size='340' side='right' caption='[[1jf6]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bvz|1bvz]], [[1jf5|1jf5]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bvz|1bvz]], [[1jf5|1jf5]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Neopullulanase Neopullulanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.135 3.2.1.135] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Neopullulanase Neopullulanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.135 3.2.1.135] </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=1jf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jf6 OCA], [http://pdbe.org/1jf6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jf6 RCSB], [http://www.ebi.ac.uk/pdbsum/1jf6 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=1jf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jf6 OCA], [http://pdbe.org/1jf6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jf6 RCSB], [http://www.ebi.ac.uk/pdbsum/1jf6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jf6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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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/jf/1jf6_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jf/1jf6_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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</div> | </div> | ||
<div class="pdbe-citations 1jf6" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1jf6" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:00, 17 January 2018
Crystal structure of thermoactinomyces vulgaris r-47 alpha-amylase mutant F286YCrystal structure of thermoactinomyces vulgaris r-47 alpha-amylase mutant F286Y
Structural highlights
Function[NEPU2_THEVU] Hydrolyzes pullulan efficiently but only a small amount of starch. Endohydrolysis of 1,4-alpha-glucosidic linkages in pullulan to form panose. Cleaves also (1-6)-alpha-glucosidic linkages to form maltotriose. 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 PubMedPhe286 located in the center of the active site of alpha-amylase 2 from Thermoactinomyces vulgaris R-47 (TVAII) plays an important role in the substrate recognition for cyclomaltooligosaccharides (cyclodextrins). The X-ray structures of mutant TVAIIs with the replacement of Phe286 by Ala (F286A) and Tyr (F286Y) were determined at 3.2 A resolution. Their structures have no significant differences from that of the wild-type enzyme. The kinetic analyses of Phe286-replaced variants showed that the variants with non-aromatic residues, Ala (F286A) and Leu (F286L), have lower enzymatic activities than those with aromatic residues, Tyr (F286Y) and Trp (F286W), and the replacement of Phe286 affects enzymatic activities for CDs more than those for starch. Role of Phe286 in the recognition mechanism of cyclomaltooligosaccharides (cyclodextrins) by Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII). X-ray structures of the mutant TVAIIs, F286A and F286Y, and kinetic analyses of the Phe286-replaced mutant TVAIIs.,Ohtaki A, Kondo S, Shimura Y, Tonozuka T, Sakano Y, Kamitori S Carbohydr Res. 2001 Sep 7;334(4):309-13. PMID:11527532[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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