7ntl: Difference between revisions
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<StructureSection load='7ntl' size='340' side='right'caption='[[7ntl]], [[Resolution|resolution]] 1.38Å' scene=''> | <StructureSection load='7ntl' size='340' side='right'caption='[[7ntl]], [[Resolution|resolution]] 1.38Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7ntl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[7ntl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Malbranchea_cinnamomea Malbranchea cinnamomea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NTL FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.38Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</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=7ntl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ntl OCA], [https://pdbe.org/7ntl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ntl RCSB], [https://www.ebi.ac.uk/pdbsum/7ntl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ntl 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=7ntl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ntl OCA], [https://pdbe.org/7ntl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ntl RCSB], [https://www.ebi.ac.uk/pdbsum/7ntl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ntl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A5J6BJN2_MALCI A0A5J6BJN2_MALCI] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 7ntl" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7ntl" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Malbranchea cinnamomea]] | ||
[[Category: Branden | [[Category: Branden G]] | ||
[[Category: Huttner | [[Category: Huttner S]] | ||
[[Category: Larsbrink | [[Category: Larsbrink L]] | ||
[[Category: Mazurkewich | [[Category: Mazurkewich S]] | ||
[[Category: Seveso | [[Category: Seveso A]] | ||
Revision as of 14:02, 15 November 2023
AA9 lytic polysaccharide monooxygenase (LPMO) from Malbranchea cinnamomeaAA9 lytic polysaccharide monooxygenase (LPMO) from Malbranchea cinnamomea
Structural highlights
FunctionPublication Abstract from PubMedThe thermophilic fungus Malbranchea cinnamomea contains a host of enzymes that enable its ability as an efficient degrader of plant biomass and that could be mined for industrial applications. This thermophilic fungus has been studied and found to encode eight lytic polysaccharide monooxygenases (LPMOs) from auxiliary activity family 9 (AA9), which collectively possess different substrate specificities for a range of plant cell-wall-related polysaccharides and oligosaccharides. To gain greater insight into the molecular determinants defining the different specificities, structural studies were pursued and the structure of McAA9F was determined. The enzyme contains the immunoglobulin-like fold typical of previously solved AA9 LPMO structures, but contains prominent differences in the loop regions found on the surface of the substrate-binding site. Most significantly, McAA9F has a broad substrate specificity, with activity on both crystalline and soluble polysaccharides. Moreover, it contains a small loop in a region where a large loop has been proposed to govern specificity towards oligosaccharides. The presence of the small loop leads to a considerably flatter and more open surface that is likely to enable the broad specificity of the enzyme. The enzyme contains a succinimide residue substitution, arising from intramolecular cyclization of Asp10, at a position where several homologous members contain an equivalent residue but cyclization has not previously been observed. This first structure of an AA9 LPMO from M. cinnamomea aids both the understanding of this family of enzymes and the exploration of the repertoire of industrially relevant lignocellulolytic enzymes from this fungus. Structure of a C1/C4-oxidizing AA9 lytic polysaccharide monooxygenase from the thermophilic fungus Malbranchea cinnamomea.,Mazurkewich S, Seveso A, Huttner S, Branden G, Larsbrink J Acta Crystallogr D Struct Biol. 2021 Aug 1;77(Pt 8):1019-1026. doi:, 10.1107/S2059798321006628. Epub 2021 Jul 29. PMID:34342275[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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