3wfz
From Proteopedia
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==Crystal structure of Galacto-N-Biose/Lacto-N-Biose I Phosphorylase C236Y Mutant== | ==Crystal structure of Galacto-N-Biose/Lacto-N-Biose I Phosphorylase C236Y Mutant== | ||
| - | <StructureSection load='3wfz' size='340' side='right'caption='[[3wfz]] | + | <StructureSection load='3wfz' size='340' side='right'caption='[[3wfz]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WFZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WFZ FirstGlance]. <br> |
| - | </td></tr> | + | </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=3wfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wfz OCA], [https://pdbe.org/3wfz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wfz RCSB], [https://www.ebi.ac.uk/pdbsum/3wfz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wfz ProSAT]</span></td></tr> |
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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=3wfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wfz OCA], [https://pdbe.org/3wfz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wfz RCSB], [https://www.ebi.ac.uk/pdbsum/3wfz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wfz ProSAT]</span></td></tr> | + | |
</table> | </table> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Galacto-N-biose/lacto-N-biose I phosphorylase (GLNBP) is the key enzyme in the enzymatic production of lacto-N-biose I. For the purpose of industrial use, we improved the thermostability of GLNBP by evolutionary engineering in which five substitutions in the amino acid sequence were selected from a random mutagenesis GLNBP library constructed using error-prone polymerase chain reaction. Among them, C236Y and D576V mutants showed considerably improved thermostability. Structural analysis of C236Y revealed that the hydroxyl group of Tyr236 forms a hydrogen bond with the carboxyl group of E319. The C236Y and D576V mutations together contributed to the thermostability. The C236Y/D576V mutant exhibited 20 degrees C higher thermostability than the wild type. | ||
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| - | Directed evolution to enhance thermostability of galacto-N-biose/lacto-N-biose I phosphorylase.,Koyama Y, Hidaka M, Nishimoto M, Kitaoka M Protein Eng Des Sel. 2013 Sep 24. PMID:24065834<ref>PMID:24065834</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3wfz" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Hidaka | + | [[Category: Hidaka M]] |
| - | [[Category: Kawakami | + | [[Category: Kawakami M]] |
| - | [[Category: Kitaoka | + | [[Category: Kitaoka M]] |
| - | [[Category: Koyama | + | [[Category: Koyama Y]] |
| - | [[Category: Nishimoto | + | [[Category: Nishimoto M]] |
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Revision as of 10:30, 31 August 2022
Crystal structure of Galacto-N-Biose/Lacto-N-Biose I Phosphorylase C236Y Mutant
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