6ydf: Difference between revisions
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==X-ray structure of LPMO== | ==X-ray structure of LPMO== | ||
<StructureSection load='6ydf' size='340' side='right'caption='[[6ydf]]' scene=''> | <StructureSection load='6ydf' size='340' side='right'caption='[[6ydf]], [[Resolution|resolution]] 2.12Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YDF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6YDF FirstGlance]. <br> | <table><tr><td colspan='2'>[[6ydf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Achaetomiella_virescens Achaetomiella virescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YDF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6YDF FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ydf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ydf OCA], [http://pdbe.org/6ydf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ydf RCSB], [http://www.ebi.ac.uk/pdbsum/6ydf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ydf ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aa9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1934374 Achaetomiella virescens])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ydf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ydf OCA], [http://pdbe.org/6ydf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ydf RCSB], [http://www.ebi.ac.uk/pdbsum/6ydf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ydf ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that cleave polysaccharide substrates oxidatively. First discovered because of their action on recalcitrant crystalline substrates (chitin and cellulose), a number of LPMOs are now reported to act on soluble substrates, including oligosaccharides. However, crystallographic complexes with oligosaccharides have been reported for only a single LPMO so far, an enzyme from the basidiomycete fungus Lentinus similis (LsAA9_A). Here we present a more detailed comparative study of LsAA9_A and an LPMO from the ascomycete fungus Collariella virescens (CvAA9_A) with which it shares 41.5% sequence identity. LsAA9_A is considerably more thermostable than CvAA9_A, and the structural basis for the difference has been investigated. We have compared the patterns of oligosaccharide cleavage and the patterns of binding in several new crystal structures explaining the basis for the product preferences of the two enzymes. Obtaining structural information about complexes of LPMOs with carbohydrates has proven to be very difficult in general judging from the structures reported in the literature thus far, and this can be attributed only partly to the low affinity for small substrates. We have thus evaluated the use of differential scanning fluorimetry as a guide to obtaining complex structures. Furthermore, an analysis of crystal packing of LPMOs and glycoside hydrolases corroborates the hypothesis that active site occlusion is a very significant problem for LPMO-substrate interaction analysis by crystallography, due to their relatively flat and extended substrate binding sites. | |||
Oligosaccharide Binding and Thermostability of Two Related AA9 Lytic Polysaccharide Monooxygenases.,Tandrup T, Tryfona T, Frandsen KEH, Johansen KS, Dupree P, Lo Leggio L Biochemistry. 2020 Sep 15;59(36):3347-3358. doi: 10.1021/acs.biochem.0c00312., Epub 2020 Aug 27. PMID:32818374<ref>PMID:32818374</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ydf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Achaetomiella virescens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Dupree P]] | [[Category: Dupree, P]] | ||
[[Category: Frandsen | [[Category: Frandsen, K E.H]] | ||
[[Category: Johansen | [[Category: Johansen, K S]] | ||
[[Category: | [[Category: Leggio, L Lo]] | ||
[[Category: Tandrup T]] | [[Category: Tandrup, T]] | ||
[[Category: Tryfona T]] | [[Category: Tryfona, T]] | ||
[[Category: Lytic polysaccharide monooxygenase]] | |||
[[Category: Metal binding protein]] | |||
Revision as of 14:32, 23 September 2020
X-ray structure of LPMOX-ray structure of LPMO
Structural highlights
Publication Abstract from PubMedLytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that cleave polysaccharide substrates oxidatively. First discovered because of their action on recalcitrant crystalline substrates (chitin and cellulose), a number of LPMOs are now reported to act on soluble substrates, including oligosaccharides. However, crystallographic complexes with oligosaccharides have been reported for only a single LPMO so far, an enzyme from the basidiomycete fungus Lentinus similis (LsAA9_A). Here we present a more detailed comparative study of LsAA9_A and an LPMO from the ascomycete fungus Collariella virescens (CvAA9_A) with which it shares 41.5% sequence identity. LsAA9_A is considerably more thermostable than CvAA9_A, and the structural basis for the difference has been investigated. We have compared the patterns of oligosaccharide cleavage and the patterns of binding in several new crystal structures explaining the basis for the product preferences of the two enzymes. Obtaining structural information about complexes of LPMOs with carbohydrates has proven to be very difficult in general judging from the structures reported in the literature thus far, and this can be attributed only partly to the low affinity for small substrates. We have thus evaluated the use of differential scanning fluorimetry as a guide to obtaining complex structures. Furthermore, an analysis of crystal packing of LPMOs and glycoside hydrolases corroborates the hypothesis that active site occlusion is a very significant problem for LPMO-substrate interaction analysis by crystallography, due to their relatively flat and extended substrate binding sites. Oligosaccharide Binding and Thermostability of Two Related AA9 Lytic Polysaccharide Monooxygenases.,Tandrup T, Tryfona T, Frandsen KEH, Johansen KS, Dupree P, Lo Leggio L Biochemistry. 2020 Sep 15;59(36):3347-3358. doi: 10.1021/acs.biochem.0c00312., Epub 2020 Aug 27. PMID:32818374[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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