3ukf: Difference between revisions

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<StructureSection load='3ukf' size='340' side='right'caption='[[3ukf]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='3ukf' size='340' side='right'caption='[[3ukf]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ukf]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspfm Aspfm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UKF FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ukf]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UKF FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FDA:DIHYDROFLAVINE-ADENINE+DINUCLEOTIDE'>FDA</scene>, <scene name='pdbligand=GDU:GALACTOSE-URIDINE-5-DIPHOSPHATE'>GDU</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]] 2.5&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FDA:DIHYDROFLAVINE-ADENINE+DINUCLEOTIDE'>FDA</scene>, <scene name='pdbligand=GDU:GALACTOSE-URIDINE-5-DIPHOSPHATE'>GDU</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3uka|3uka]], [[3ukh|3ukh]], [[3ukk|3ukk]], [[3ukl|3ukl]], [[3ukp|3ukp]], [[3ukq|3ukq]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glf, glfA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=746128 ASPFM])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/UDP-galactopyranose_mutase UDP-galactopyranose mutase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.9 5.4.99.9] </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=3ukf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ukf OCA], [https://pdbe.org/3ukf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ukf RCSB], [https://www.ebi.ac.uk/pdbsum/3ukf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ukf 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=3ukf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ukf OCA], [https://pdbe.org/3ukf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ukf RCSB], [https://www.ebi.ac.uk/pdbsum/3ukf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ukf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GLFA_ASPFM GLFA_ASPFM] UDP-galactopyranose mutase, key flavoenzyme of galactofuranose metabolism that catalyzes the 6-to-5 ring contraction of UDP-galactopyranose to UDP-galactofuranose, the donor used by various galacto-furanosyltransferases (PubMed:16207086, PubMed:18552284, PubMed:22334662, PubMed:23036087, PubMed:25412209, PubMed:26836146). Controls the biosynthesis of galactomannan and galactofuranose containing glycoconjugates (PubMed:18552284). The flavin functions as nucleophile, forming a flavin-sugar adduct that facilitates galactose-ring opening and contraction (PubMed:26836146). The binding of UDP-galactopyranose induces profound conformational changes in the enzyme and two loops on opposite sides of the active site move toward each other by over 10 Angstroms to cover the substrate and create a closed active site (PubMed:22334662).<ref>PMID:16207086</ref> <ref>PMID:18552284</ref> <ref>PMID:22334662</ref> <ref>PMID:23036087</ref> <ref>PMID:25412209</ref> <ref>PMID:26836146</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: Aspfm]]
[[Category: Aspergillus fumigatus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: UDP-galactopyranose mutase]]
[[Category: Sanders DAR]]
[[Category: Sanders, D A.R]]
[[Category: Van Straaten KE]]
[[Category: Straaten, K E.Van]]
[[Category: Fadh2]]
[[Category: Flavoenzyme]]
[[Category: Isomerase]]
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