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| | <StructureSection load='3wfz' size='340' side='right'caption='[[3wfz]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='3wfz' size='340' side='right'caption='[[3wfz]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wfz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bifl2 Bifl2]. 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> | + | <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='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> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2zuu|2zuu]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BLLJ_1623, lnpA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=565042 BIFL2])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/1,3-beta-galactosyl-N-acetylhexosamine_phosphorylase 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.211 2.4.1.211] </span></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> | | <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> |
| | + | == 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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase]] | + | [[Category: Bifidobacterium longum subsp. longum JCM 1217]] |
| - | [[Category: Bifl2]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hidaka, M]] | + | [[Category: Hidaka M]] |
| - | [[Category: Kawakami, M]] | + | [[Category: Kawakami M]] |
| - | [[Category: Kitaoka, M]] | + | [[Category: Kitaoka M]] |
| - | [[Category: Koyama, Y]] | + | [[Category: Koyama Y]] |
| - | [[Category: Nishimoto, M]] | + | [[Category: Nishimoto M]] |
| - | [[Category: Beta-alpha-barrel]]
| + | |
| - | [[Category: Phosphorylase]]
| + | |
| - | [[Category: Tim barrel]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
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.[1] [2] [3]
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kitaoka M, Tian J, Nishimoto M. Novel putative galactose operon involving lacto-N-biose phosphorylase in Bifidobacterium longum. Appl Environ Microbiol. 2005 Jun;71(6):3158-62. PMID:15933016 doi:71/6/3158
- ↑ Nishimoto M, Kitaoka M. Identification of N-acetylhexosamine 1-kinase in the complete lacto-N-biose I/galacto-N-biose metabolic pathway in Bifidobacterium longum. Appl Environ Microbiol. 2007 Oct;73(20):6444-9. Epub 2007 Aug 24. PMID:17720833 doi:http://dx.doi.org/10.1128/AEM.01425-07
- ↑ Hidaka M, Nishimoto M, Kitaoka M, Wakagi T, Shoun H, Fushinobu S. The crystal structure of galacto-N-biose/lacto-N-biose I phosphorylase: a large deformation of a TIM barrel scaffold. J Biol Chem. 2009 Mar 13;284(11):7273-83. Epub 2009 Jan 5. PMID:19124470 doi:10.1074/jbc.M808525200
- ↑ Koyama Y, Hidaka M, Nishimoto M, Kitaoka M. Directed evolution to enhance thermostability of galacto-N-biose/lacto-N-biose I phosphorylase. Protein Eng Des Sel. 2013 Sep 24. PMID:24065834 doi:http://dx.doi.org/10.1093/protein/gzt049
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