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6h1z
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==AFGH61B WILD-TYPE== | |
| + | <StructureSection load='6h1z' size='340' side='right' caption='[[6h1z]], [[Resolution|resolution]] 1.57Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6h1z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfu Aspfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H1Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H1Z FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AFUA_4G07850 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=330879 ASPFU])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6h1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h1z OCA], [http://pdbe.org/6h1z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h1z RCSB], [http://www.ebi.ac.uk/pdbsum/6h1z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h1z ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Lytic polysaccharide monooxygenases (LPMOs) are industrial enzymes which are gaining use in second generation bioethanol production from lignocellulose by acting in synergy with glycoside hydrolases. Here we present the X-ray crystal structure of an AA9 fungal LPMO from Aspergillus fumigatus and a variant which has been shown to have better performance at elevated temperatures. Based on the structures, thermal denaturation data and theoretical calculations, we provide a suggestion for the structural basis of the improved stability. | ||
| - | + | Structure of a lytic polysaccharide monooxygenase from Aspergillus fumigatus and an engineered thermostable variant.,Lo Leggio L, Weihe CD, Poulsen JN, Sweeney M, Rasmussen F, Lin J, De Maria L, Wogulis M Carbohydr Res. 2018 Nov;469:55-59. doi: 10.1016/j.carres.2018.08.009. Epub 2018, Aug 14. PMID:30296642<ref>PMID:30296642</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Poulsen, J | + | <div class="pdbe-citations 6h1z" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aspfu]] | ||
| + | [[Category: Leggio, L Lo]] | ||
| + | [[Category: Poulsen, J C.N]] | ||
| + | [[Category: Lytic polysaccharide monooxygenase]] | ||
| + | [[Category: Oxidoreductase]] | ||
Current revision
AFGH61B WILD-TYPE
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