6ibi: Difference between revisions
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<StructureSection load='6ibi' size='340' side='right'caption='[[6ibi]], [[Resolution|resolution]] 2.08Å' scene=''> | <StructureSection load='6ibi' size='340' side='right'caption='[[6ibi]], [[Resolution|resolution]] 2.08Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6ibi]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IBI OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6ibi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Laetisaria_arvalis Laetisaria arvalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IBI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IBI FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.08Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=6ibi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ibi OCA], [https://pdbe.org/6ibi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ibi RCSB], [https://www.ebi.ac.uk/pdbsum/6ibi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ibi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/X325_WAIAR X325_WAIAR] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Lytic polysaccharide monooxygenases (LPMOs) are copper-containing enzymes that play a key role in the oxidative degradation of various biopolymers such as cellulose and chitin. While hunting for new LPMOs, we identified a new family of proteins, defined here as X325, in various fungal lineages. The three-dimensional structure of X325 revealed an overall LPMO fold and a His brace with an additional Asp ligand to Cu(II). Although LPMO-type activity of X325 members was initially expected, we demonstrated that X325 members do not perform oxidative cleavage of polysaccharides, establishing that X325s are not LPMOs. Investigations of the biological role of X325 in the ectomycorrhizal fungus Laccaria bicolor revealed exposure of the X325 protein at the interface between fungal hyphae and tree rootlet cells. Our results provide insights into a family of copper-containing proteins, which is widespread in the fungal kingdom and is evolutionarily related to LPMOs, but has diverged to biological functions other than polysaccharide degradation. | |||
A fungal family of lytic polysaccharide monooxygenase-like copper proteins.,Labourel A, Frandsen KEH, Zhang F, Brouilly N, Grisel S, Haon M, Ciano L, Ropartz D, Fanuel M, Martin F, Navarro D, Rosso MN, Tandrup T, Bissaro B, Johansen KS, Zerva A, Walton PH, Henrissat B, Leggio LL, Berrin JG Nat Chem Biol. 2020 Jan 13. pii: 10.1038/s41589-019-0438-8. doi:, 10.1038/s41589-019-0438-8. PMID:31932718<ref>PMID:31932718</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ibi" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Laetisaria arvalis]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Berrin | [[Category: Berrin J-G]] | ||
[[Category: Frandsen | [[Category: Frandsen KEH]] | ||
[[Category: Haon | [[Category: Haon M]] | ||
[[Category: Labourel | [[Category: Labourel A]] | ||
[[Category: Leggio | [[Category: Lo Leggio L]] | ||
[[Category: Tandrup | [[Category: Tandrup T]] | ||
Latest revision as of 13:03, 23 October 2024
Copper binding protein from Laetisaria arvalis (LaX325)Copper binding protein from Laetisaria arvalis (LaX325)
Structural highlights
FunctionPublication Abstract from PubMedLytic polysaccharide monooxygenases (LPMOs) are copper-containing enzymes that play a key role in the oxidative degradation of various biopolymers such as cellulose and chitin. While hunting for new LPMOs, we identified a new family of proteins, defined here as X325, in various fungal lineages. The three-dimensional structure of X325 revealed an overall LPMO fold and a His brace with an additional Asp ligand to Cu(II). Although LPMO-type activity of X325 members was initially expected, we demonstrated that X325 members do not perform oxidative cleavage of polysaccharides, establishing that X325s are not LPMOs. Investigations of the biological role of X325 in the ectomycorrhizal fungus Laccaria bicolor revealed exposure of the X325 protein at the interface between fungal hyphae and tree rootlet cells. Our results provide insights into a family of copper-containing proteins, which is widespread in the fungal kingdom and is evolutionarily related to LPMOs, but has diverged to biological functions other than polysaccharide degradation. A fungal family of lytic polysaccharide monooxygenase-like copper proteins.,Labourel A, Frandsen KEH, Zhang F, Brouilly N, Grisel S, Haon M, Ciano L, Ropartz D, Fanuel M, Martin F, Navarro D, Rosso MN, Tandrup T, Bissaro B, Johansen KS, Zerva A, Walton PH, Henrissat B, Leggio LL, Berrin JG Nat Chem Biol. 2020 Jan 13. pii: 10.1038/s41589-019-0438-8. doi:, 10.1038/s41589-019-0438-8. PMID:31932718[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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