| Structural highlights
8b4g is a 1 chain structure with sequence from Thermoascus aurantiacus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.496Å |
| Ligands: | 2HA, AKR, CL, CU, HIC, NAG |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
LP9A_THEAU Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation product (PubMed:21876164, PubMed:29971843, Ref.4). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (PubMed:21876164, PubMed:29971843, Ref.4). Is able to cleave cellulose and xylan to produce C1- and C4-oxidized products (Ref.4).[1] [2] [3]
References
- ↑ Quinlan RJ, Sweeney MD, Lo Leggio L, Otten H, Poulsen JC, Johansen KS, Krogh KB, Jorgensen CI, Tovborg M, Anthonsen A, Tryfona T, Walter CP, Dupree P, Xu F, Davies GJ, Walton PH. Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components. Proc Natl Acad Sci U S A. 2011 Sep 13;108(37):15079-84. Epub 2011 Aug 29. PMID:21876164 doi:10.1073/pnas.1105776108
- ↑ Petrović DM, Bissaro B, Chylenski P, Skaugen M, Sørlie M, Jensen MS, Aachmann FL, Courtade G, Várnai A, Eijsink VGH. Methylation of the N-terminal histidine protects a lytic polysaccharide monooxygenase from auto-oxidative inactivation. Protein Sci. 2018 Sep;27(9):1636-1650. PMID:29971843 doi:10.1002/pro.3451
- ↑ Banerjee S, Muderspach SJ, Tandrup T, Frandsen KEH, Singh RK, Ipsen JØ, Hernández-Rollán C, Nørholm MHH, Bjerrum MJ, Johansen KS, Lo Leggio L. Protonation State of an Important Histidine from High Resolution Structures of Lytic Polysaccharide Monooxygenases. Biomolecules. 2022 Jan 24;12(2):194. PMID:35204695 doi:10.3390/biom12020194
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