|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6yde' size='340' side='right'caption='[[6yde]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='6yde' size='340' side='right'caption='[[6yde]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6yde]] is a 1 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=6YDE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6YDE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6yde]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Collariella_virescens Collariella virescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YDE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YDE FirstGlance]. <br> |
| - | </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=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></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=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=PRD_900020:beta-cellohexaose'>PRD_900020</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'>[https://proteopedia.org/fgij/fg.htm?mol=6yde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yde OCA], [https://pdbe.org/6yde PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yde RCSB], [https://www.ebi.ac.uk/pdbsum/6yde PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yde ProSAT]</span></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=6yde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yde OCA], [http://pdbe.org/6yde PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6yde RCSB], [http://www.ebi.ac.uk/pdbsum/6yde PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6yde ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A223GEC9_9PEZI A0A223GEC9_9PEZI] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 18: |
Line 19: |
| | </div> | | </div> |
| | <div class="pdbe-citations 6yde" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6yde" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Monooxygenase 3D structures|Monooxygenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Achaetomiella virescens]] | + | [[Category: Collariella virescens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dupree, P]] | + | [[Category: Dupree P]] |
| - | [[Category: Frandsen, K E.H]] | + | [[Category: Frandsen KEH]] |
| - | [[Category: Johansen, K S]] | + | [[Category: Johansen KS]] |
| - | [[Category: Leggio, L Lo]] | + | [[Category: Lo Leggio L]] |
| - | [[Category: Tandrup, T]] | + | [[Category: Tandrup T]] |
| - | [[Category: Tryfona, T]] | + | [[Category: Tryfona T]] |
| - | [[Category: Cellohexaose]]
| + | |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Lytic polysaccharide monooxygenase]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| Structural highlights
6yde is a 1 chain structure with sequence from Collariella virescens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.2Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
A0A223GEC9_9PEZI
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tandrup T, Tryfona T, Frandsen KEH, Johansen KS, Dupree P, Lo Leggio L. Oligosaccharide Binding and Thermostability of Two Related AA9 Lytic Polysaccharide Monooxygenases. Biochemistry. 2020 Sep 15;59(36):3347-3358. doi: 10.1021/acs.biochem.0c00312., Epub 2020 Aug 27. PMID:32818374 doi:http://dx.doi.org/10.1021/acs.biochem.0c00312
|
