7pu1

High resolution X-ray structure of Thermoascus aurantiacus LPMO

spinqualitylabelsall models 7pu1, resolution 1.06Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7pu1 is a 2 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 1.06Å Ligands: CL, CU, HIC, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G3XAP7_THEAU Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds. Involved in the degradation of complex natural cellulosic substrates.[RuleBase:RU368122] Publication Abstract from PubMed Lytic Polysaccharide Monooxygenases (LPMOs) oxidatively cleave recalcitrant polysaccharides. The mechanism involves (i) reduction of the Cu, (ii) polysaccharide binding, (iii) binding of different oxygen species, and (iv) glycosidic bond cleavage. However, the complete mechanism is poorly understood and may vary across different families and even within the same family. Here, we have investigated the protonation state of a secondary co-ordination sphere histidine, conserved across AA9 family LPMOs that has previously been proposed to be a potential proton donor. Partial unrestrained refinement of newly obtained higher resolution data for two AA9 LPMOs and re-refinement of four additional data sets deposited in the PDB were carried out, where the His was refined without restraints, followed by measurements of the His ring geometrical parameters. This allowed reliable assignment of the protonation state, as also validated by following the same procedure for the His brace, for which the protonation state is predictable. The study shows that this histidine is generally singly protonated at the Nepsilon2 atom, which is close to the oxygen species binding site. Our results indicate robustness of the method. In view of this and other emerging evidence, a role as proton donor during catalysis is unlikely for this His. Protonation State of an Important Histidine from High Resolution Structures of Lytic Polysaccharide Monooxygenases.,Banerjee S, Muderspach SJ, Tandrup T, Frandsen KEH, Singh RK, Ipsen JO, Hernandez-Rollan C, Norholm MHH, Bjerrum MJ, Johansen KS, Lo Leggio L Biomolecules. 2022 Jan 24;12(2). pii: biom12020194. doi: 10.3390/biom12020194. PMID:35204695 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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