{"title":"1H, 13C and 15N backbone resonance assignment of the lytic polysaccharide monooxygenase LsAA9A from Lentinus similis","authors":"Piera Wiesinger, Mats Sandgren, Gustav Nestor","doi":"10.1007/s12104-025-10256-z","DOIUrl":null,"url":null,"abstract":"<div><p>Lytic polysaccharide monooxygenases (LPMOs) are mono-copper binding enzymes involved in the degradation of carbohydrates. The 25 kDa sized LPMO <i>Ls</i>AA9A from the basidiomycete <i>Lentinus similis</i> is known to oxidate cellulose and cellooligomers at the C4 position and thus leading to a breakage of the glycosidic bond. <i>Ls</i>AA9A has been recombinantly expressed in <i>Escherichia coli</i> with <sup>13</sup>C and <sup>15</sup>N labelling. Here, we present the <sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N backbone resonance assignment of the <i>apo</i> form. The secondary structure was predicted using the TALOS-N software and it was overall in agreement with the crystal structure of <i>Ls</i>AA9A expressed in <i>E. coli</i>. A few shorter α-helices and β-sheets present in the crystal structure are missing in the NMR prediction and vice versa. <i>Ls</i>AA9A resembles the typical structural elements of LPMOs with a core β-sandwich.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.5000,"publicationDate":"2025-11-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s12104-025-10256-z.pdf","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biomolecular NMR Assignments","FirstCategoryId":"99","ListUrlMain":"https://link.springer.com/article/10.1007/s12104-025-10256-z","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOPHYSICS","Score":null,"Total":0}
引用次数: 0
Abstract
Lytic polysaccharide monooxygenases (LPMOs) are mono-copper binding enzymes involved in the degradation of carbohydrates. The 25 kDa sized LPMO LsAA9A from the basidiomycete Lentinus similis is known to oxidate cellulose and cellooligomers at the C4 position and thus leading to a breakage of the glycosidic bond. LsAA9A has been recombinantly expressed in Escherichia coli with 13C and 15N labelling. Here, we present the 1H, 13C and 15N backbone resonance assignment of the apo form. The secondary structure was predicted using the TALOS-N software and it was overall in agreement with the crystal structure of LsAA9A expressed in E. coli. A few shorter α-helices and β-sheets present in the crystal structure are missing in the NMR prediction and vice versa. LsAA9A resembles the typical structural elements of LPMOs with a core β-sandwich.
期刊介绍：
Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties.
Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.
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