3wfz: Difference between revisions
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==Crystal structure of Galacto-N-Biose/Lacto-N-Biose I Phosphorylase C236Y Mutant== | |||
<StructureSection load='3wfz' size='340' side='right'caption='[[3wfz]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3wfz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bifidobacterium_longum_subsp._longum_JCM_1217 Bifidobacterium longum subsp. longum JCM 1217]. 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><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></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> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/LNPA_BIFL2 LNPA_BIFL2] Reversibly phosphorolyzes lacto-N-biose to Gal1-P and N-acetylglucosamine (GlcNAc) and galacto-N-biose to Gal1-P and N-acetylgalactosamine (GalNAc). Involved in the lacto-N-biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is important for host intestinal colonization by bifidobacteria.<ref>PMID:15933016</ref> <ref>PMID:17720833</ref> <ref>PMID:19124470</ref> | |||
<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. | |||
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> | |||
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__ | |||
</StructureSection> | |||
[[Category: Bifidobacterium longum subsp. longum JCM 1217]] | |||
[[Category: Large Structures]] | |||
[[Category: Hidaka M]] | |||
[[Category: Kawakami M]] | |||
[[Category: Kitaoka M]] | |||
[[Category: Koyama Y]] | |||
[[Category: Nishimoto M]] | |||
Latest revision as of 13:08, 8 November 2023
Crystal structure of Galacto-N-Biose/Lacto-N-Biose I Phosphorylase C236Y Mutant
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