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7PYZ

Structure of LPMO (expressed in E.coli) with cellotriose at 2.97x10^6 Gy

Summary for 7PYZ
Entry DOI10.2210/pdb7pyz/pdb
Related7PQR 7PXI 7PXJ 7PXK 7PXL 7PXM 7PXN 7PXR 7PXS 7PXT 7PXU 7PXV 7PXW 7PYD 7PYE 7PYF 7PYG 7PYH 7PYI 7PYL 7PYM 7PYN 7PYO 7PYP 7PYQ
Related PRD IDPRD_900021
DescriptorAuxiliary activity 9, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, COPPER (II) ION, ... (6 entities in total)
Functional Keywordslytic polysaccharide monooxygenase, metalloenzyme, copper, auxiliary activity, oxidoreductase
Biological sourcePanus similis
Total number of polymer chains1
Total formula weight26151.46
Authors
Tandrup, T.,Muderspach, S.J.,Banerjee, S.,Ipsen, J.O.,Rollan, C.H.,Norholm, M.H.H.,Johansen, K.S.,Lo Leggio, L. (deposition date: 2021-10-11, release date: 2022-08-24, Last modification date: 2024-11-13)
Primary citationTandrup, T.,Muderspach, S.J.,Banerjee, S.,Santoni, G.,Ipsen, J.O.,Hernandez-Rollan, C.,Norholm, M.H.H.,Johansen, K.S.,Meilleur, F.,Lo Leggio, L.
Changes in active-site geometry on X-ray photoreduction of a lytic polysaccharide monooxygenase active-site copper and saccharide binding.
Iucrj, 9:666-681, 2022
Cited by
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 to Cu. Here we have used a systematic diffraction data collection method to monitor structural changes in two AA9 LPMOs, one from (AA9_A) and one from (AA9_A), as the active-site Cu is photoreduced in the X-ray beam. For 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 photoreduction. We can recommend that crystallographic studies of AA9 LPMOs wishing to address the Cu form use a total X-ray dose below 3 × 10 Gy, while the Cu form can be attained using 1 × 10 Gy. In all cases, we observe the transition from a hexa-coordinated Cu site with two solvent-facing ligands to a T-shaped geometry with no exogenous ligands, and a clear increase of the θ parameter and a decrease of the θ parameter by averages of 9.2° and 8.4°, respectively, but also a slight increase in θ. Thus, the θ and θ parameters are helpful diagnostics for the oxidation state of the metal in a His-brace protein. On binding of cello-oligosaccharides to AA9_A, regardless of the production source, the θ parameter increases, making the Cu site less planar, while the active-site Tyr-Cu distance decreases reproducibly for the Cu form. Thus, the θ increase found on copper reduction may bring AA9_A closer to an oligosaccharide-bound state and contribute to the observed higher affinity of reduced AA9_A for cellulosic substrates.
PubMed: 36071795
DOI: 10.1107/S2052252522007175
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

227561

数据于2024-11-20公开中

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