Summary for 5UIZ
| Entry DOI | 10.2210/pdb5uiz/pdb |
| Descriptor | AA10A, COPPER (II) ION, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | aa10a, polysaccharide monooxygenase, oxidoreductase, e7, lpmo, lyase |
| Biological source | Thermobifida fusca |
| Total number of polymer chains | 2 |
| Total formula weight | 54573.13 |
| Authors | Alahuhta, P.M.,Lunin, V.V. (deposition date: 2017-01-16, release date: 2017-02-01, Last modification date: 2024-10-23) |
| Primary citation | Kruer-Zerhusen, N.,Alahuhta, M.,Lunin, V.V.,Himmel, M.E.,Bomble, Y.J.,Wilson, D.B. Structure of a Thermobifida fusca lytic polysaccharide monooxygenase and mutagenesis of key residues. Biotechnol Biofuels, 10:243-243, 2017 Cited by PubMed Abstract: Auxiliary activity (AA) enzymes are produced by numerous bacterial and fungal species to assist in the degradation of biomass. These enzymes are abundant but have yet to be fully characterized. Here, we report the X-ray structure of AA10A (TfAA10A), investigate mutational characterization of key surface residues near its active site, and explore the importance of the various domains of AA10B (TfAA10B). The structure of TfAA10A is similar to other bacterial LPMOs (lytic polysaccharide monooxygenases), including signs of photo-reduction and a distorted active site, with mixed features showing both type I and II copper coordination. The point mutation experiments of TfAA10A show that Trp82 and Asn83 are needed for binding, but only Trp82 affects activity. The TfAA10B domain truncation mutants reveal that CBM2 is crucial for the binding of substrate, but that the X1 module does not affect binding or activity. PubMed: 29213309DOI: 10.1186/s13068-017-0925-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report
