6yjo

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Current revision (10:45, 23 October 2024) (edit) (undo)
 
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<StructureSection load='6yjo' size='340' side='right'caption='[[6yjo]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
<StructureSection load='6yjo' size='340' side='right'caption='[[6yjo]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6yjo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_graminearum_PH-1 Fusarium graminearum PH-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YJO FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YJO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.38&#8491;</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]] 2.38&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=6yjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yjo OCA], [https://pdbe.org/6yjo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yjo RCSB], [https://www.ebi.ac.uk/pdbsum/6yjo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yjo ProSAT]</span></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=6yjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yjo OCA], [https://pdbe.org/6yjo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yjo RCSB], [https://www.ebi.ac.uk/pdbsum/6yjo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yjo ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
 
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[https://www.uniprot.org/uniprot/A0A098DND1_GIBZE A0A098DND1_GIBZE]
 
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Oxidative plant cell-wall processing enzymes are of great importance in biology and biotechnology. Yet, our insight into the functional interplay amongst such oxidative enzymes remains limited. Here, a phylogenetic analysis of the auxiliary activity 7 family (AA7), currently harbouring oligosaccharide flavo-oxidases, reveals a striking abundance of AA7-genes in phytopathogenic fungi and Oomycetes. Expression of five fungal enzymes, including three from unexplored clades, expands the AA7-substrate range and unveils a cellooligosaccharide dehydrogenase activity, previously unknown within AA7. Sequence and structural analyses identify unique signatures distinguishing the strict dehydrogenase clade from canonical AA7 oxidases. The discovered dehydrogenase directly is able to transfer electrons to an AA9 lytic polysaccharide monooxygenase (LPMO) and fuel cellulose degradation by LPMOs without exogenous reductants. The expansion of redox-profiles and substrate range highlights the functional diversity within AA7 and sets the stage for harnessing AA7 dehydrogenases to fine-tune LPMO activity in biotechnological conversion of plant feedstocks.
 
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Discovery of fungal oligosaccharide-oxidising flavo-enzymes with previously unknown substrates, redox-activity profiles and interplay with LPMOs.,Haddad Momeni M, Fredslund F, Bissaro B, Raji O, Vuong TV, Meier S, Nielsen TS, Lombard V, Guigliarelli B, Biaso F, Haon M, Grisel S, Henrissat B, Welner DH, Master ER, Berrin JG, Abou Hachem M Nat Commun. 2021 Apr 9;12(1):2132. doi: 10.1038/s41467-021-22372-0. PMID:33837197<ref>PMID:33837197</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 6yjo" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Fusarium graminearum PH-1]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Abou Hachem M]]
 
[[Category: Berrin JG]]
[[Category: Berrin JG]]
[[Category: Fredslund F]]
[[Category: Fredslund F]]
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[[Category: Haddad Momeni M]]
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[[Category: Hachem MA]]
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[[Category: Momeni MH]]
[[Category: Welner DH]]
[[Category: Welner DH]]

Current revision

Structure of FgChi7B

PDB ID 6yjo

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