5lsv: Difference between revisions
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==X-ray crystal structure of AA13 LPMO== | ==X-ray crystal structure of AA13 LPMO== | ||
<StructureSection load='5lsv' size='340' side='right' caption='[[5lsv]], [[Resolution|resolution]] 1.10Å' scene=''> | <StructureSection load='5lsv' size='340' side='right'caption='[[5lsv]], [[Resolution|resolution]] 1.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5lsv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LSV OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5lsv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_oryzae_RIB40 Aspergillus oryzae RIB40]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LSV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LSV FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand= | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.1Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5lsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lsv OCA], [https://pdbe.org/5lsv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lsv RCSB], [https://www.ebi.ac.uk/pdbsum/5lsv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lsv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/AA13_ASPOR AA13_ASPOR] Lytic polysaccharide monooxygenase-related protein that has no activity towards starch.<ref>PMID:25608804</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 17: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 5lsv" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5lsv" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Aspergillus oryzae RIB40]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Frandsen KEH]] | ||
[[Category: | [[Category: Johansen KS]] | ||
[[Category: | [[Category: Lo Leggio L]] | ||
[[Category: | [[Category: Poulsen J-CN]] | ||
[[Category: | [[Category: Tovborg M]] | ||
Latest revision as of 21:46, 18 October 2023
X-ray crystal structure of AA13 LPMOX-ray crystal structure of AA13 LPMO
Structural highlights
FunctionAA13_ASPOR Lytic polysaccharide monooxygenase-related protein that has no activity towards starch.[1] Publication Abstract from PubMedLytic polysaccharide monooxygenases (LPMOs) are a class of copper-dependent enzymes discovered within the last ten years. They oxidatively cleave polysaccharides (chitin, lignocellulose, hemicellulose and starch-derived), presumably making recalcitrant substrates accessible to glycoside hydrolases. Recently, the first crystal structure of an LPMO-substrate complex was reported, giving insights into the interaction of LPMOs with beta-linked substrates (Frandsen et al., 2016). The LPMOs acting on alpha-linked glycosidic bonds (family AA13) display binding surfaces that are quite different from those of LPMOs that act on beta-linked glycosidic bonds (families AA9-AA11), as revealed from the first determined structure (Lo Leggio et al., 2015), and thus presumably the AA13s interact with their substrate in a distinct fashion. Here, several new structures of the same AA13 enzyme, Aspergillus oryzae AA13, are presented. Crystals obtained in the presence of high zinc-ion concentrations were used, as they can be obtained more reproducibly than those used to refine the deposited copper-containing structure. One structure with an ordered zinc-bound active site was solved at 1.65 A resolution, and three structures from crystals soaked with maltooligosaccharides in solutions devoid of zinc ions were solved at resolutions of up to 1.10 A. Despite similar unit-cell parameters, small rearrangements in the crystal packing occur when the crystals are depleted of zinc ions, resulting in a more occluded substrate-binding surface. In two of the three structures maltooligosaccharide ligands are bound, but not at the active site. Two of the structures presented show a His-ligand conformation that is incompatible with metal-ion binding. In one of these structures this conformation is the principal one (80% occupancy), giving a rare atomic resolution view of a substantially misfolded enzyme that is presumably rendered inactive. Learning from oligosaccharide soaks of crystals of an AA13 lytic polysaccharide monooxygenase: crystal packing, ligand binding and active-site disorder.,Frandsen KE, Poulsen JC, Tovborg M, Johansen KS, Lo Leggio L Acta Crystallogr D Struct Biol. 2017 Jan 1;73(Pt 1):64-76. doi:, 10.1107/S2059798316019641. Epub 2017 Jan 1. PMID:28045386[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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