5acf: Difference between revisions
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<StructureSection load='5acf' size='340' side='right'caption='[[5acf]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='5acf' size='340' side='right'caption='[[5acf]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5acf]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5acf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Panus_similis Panus similis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ACF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ACF FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand= | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900021:beta-cellotriose'>PRD_900021</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=5acf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5acf OCA], [https://pdbe.org/5acf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5acf RCSB], [https://www.ebi.ac.uk/pdbsum/5acf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5acf ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0S2GKZ1_9APHY A0A0S2GKZ1_9APHY] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Panus similis]] | ||
[[Category: Frandsen | [[Category: Frandsen KEH]] | ||
[[Category: Johansen | [[Category: Johansen KS]] | ||
[[Category: Leggio | [[Category: Lo Leggio L]] | ||
[[Category: Poulsen | [[Category: Poulsen JN]] | ||
[[Category: Tovborg | [[Category: Tovborg M]] | ||
Revision as of 07:51, 25 May 2023
X-ray Structure of LPMOX-ray Structure of LPMO
Structural highlights
FunctionPublication Abstract from PubMedLytic polysaccharide monooxygenases (LPMOs) are copper-containing enzymes that oxidatively break down recalcitrant polysaccharides such as cellulose and chitin. Since their discovery, LPMOs have become integral factors in the industrial utilization of biomass, especially in the sustainable generation of cellulosic bioethanol. We report here a structural determination of an LPMO-oligosaccharide complex, yielding detailed insights into the mechanism of action of these enzymes. Using a combination of structure and electron paramagnetic resonance spectroscopy, we reveal the means by which LPMOs interact with saccharide substrates. We further uncover electronic and structural features of the enzyme active site, showing how LPMOs orchestrate the reaction of oxygen with polysaccharide chains. The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases.,Frandsen KE, Simmons TJ, Dupree P, Poulsen JN, Hemsworth GR, Ciano L, Johnston EM, Tovborg M, Johansen KS, von Freiesleben P, Marmuse L, Fort S, Cottaz S, Driguez H, Henrissat B, Lenfant N, Tuna F, Baldansuren A, Davies GJ, Lo Leggio L, Walton PH Nat Chem Biol. 2016 Feb 29. doi: 10.1038/nchembio.2029. PMID:26928935[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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