{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Tandrup T"],"funding":["Danish Council for Independent Research","BioStruct-X","Danish Ministry of Higher Education and Science","Novo Nordisk Foundation HOPE project","NNF Center for Biosustainability","Novo Nordisk Fonden","Seventh Framework Programme of the European Community"],"pagination":["666-681"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9438499"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["9(Pt 5)"],"pubmed_abstract":["The recently discovered lytic polysaccharide monooxygenases (LPMOs) are Cu-containing enzymes capable of degrading polysaccharide substrates oxidatively. The generally accepted first step in the LPMO reaction is the reduction of the active-site metal ion from Cu<sup>2+</sup> to Cu<sup>+</sup>. Here we have used a systematic diffraction data collection method to monitor structural changes in two AA9 LPMOs, one from <i>Lentinus similis</i> (<i>Ls</i>AA9_A) and one from <i>Thermoascus auranti-acus</i> (<i>Ta</i>AA9_A), as the active-site Cu is photoreduced in the X-ray beam. For <i>Ls</i>AA9_A, the protein produced in two different recombinant systems was crystallized to probe the effect of post-translational modifications and different crystallization conditions on the active site and metal "],"journal":["IUCrJ"],"pubmed_title":["Changes in active-site geometry on X-ray photoreduction of a lytic polysaccharide monooxygenase active-site copper and saccharide binding."],"pmcid":["PMC9438499"],"funding_grant_id":["Biofoundry and Strain Design Teams","NNF17SA0027704","FP7/2007–2013","NNF10CC1016517","8021-00273B","283570"],"pubmed_authors":["Banerjee S","Lo Leggio L","Hernandez-Rollan C","Johansen KS","Meilleur F","Tandrup T","Muderspach SJ","Santoni G","Ipsen JO","Norholm MHH"],"additional_accession":[]},"is_claimable":false,"name":"Changes in active-site geometry on X-ray photoreduction of a lytic polysaccharide monooxygenase active-site copper and saccharide binding.","description":"The recently discovered lytic polysaccharide monooxygenases (LPMOs) are Cu-containing enzymes capable of degrading polysaccharide substrates oxidatively. The generally accepted first step in the LPMO reaction is the reduction of the active-site metal ion from Cu<sup>2+</sup> to Cu<sup>+</sup>. Here we have used a systematic diffraction data collection method to monitor structural changes in two AA9 LPMOs, one from <i>Lentinus similis</i> (<i>Ls</i>AA9_A) and one from <i>Thermoascus auranti-acus</i> (<i>Ta</i>AA9_A), as the active-site Cu is photoreduced in the X-ray beam. For <i>Ls</i>AA9_A, the protein produced in two different recombinant systems was crystallized to probe the effect of post-translational modifications and different crystallization conditions on the active site and metal ","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Sep","modification":"2026-05-28T06:47:20.936Z","creation":"2025-02-19T03:29:00.643Z"},"accession":"S-EPMC9438499","cross_references":{"pubmed":["36071795"],"doi":["10.1107/S2052252522007175"]}}