7OKR
Catalytic domain from the Aliivibrio salmonicida lytic polysaccharide monooxygenase AsLPMO10B
This is a non-PDB format compatible entry.
Summary for 7OKR
| Entry DOI | 10.2210/pdb7okr/pdb |
| Descriptor | Chitinase B, DI(HYDROXYETHYL)ETHER, COPPER (II) ION, ... (4 entities in total) |
| Functional Keywords | lpmo, lytic polysaccharide monooxygenase, aliivibrio salmonicida, chitinase, oxidoreductase |
| Biological source | Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain LFI1238)) |
| Total number of polymer chains | 1 |
| Total formula weight | 44191.14 |
| Authors | Cordara, G.,Leitl, K.D.,Loose, J.S.M.,Vaaje-Kolstad, G.,Krengel, U. (deposition date: 2021-05-18, release date: 2022-06-01, Last modification date: 2024-10-09) |
| Primary citation | Skane, A.,Edvardsen, P.K.,Cordara, G.,Loose, J.S.M.,Leitl, K.D.,Krengel, U.,Sorum, H.,Askarian, F.,Vaaje-Kolstad, G. Chitinolytic enzymes contribute to the pathogenicity of Aliivibrio salmonicida LFI1238 in the invasive phase of cold-water vibriosis. Bmc Microbiol., 22:194-194, 2022 Cited by PubMed Abstract: Aliivibrio salmonicida is the causative agent of cold-water vibriosis in salmonids (Oncorhynchus mykiss and Salmo salar L.) and gadidae (Gadus morhua L.). Virulence-associated factors that are essential for the full spectrum of A. salmonicida pathogenicity are largely unknown. Chitin-active lytic polysaccharide monooxygenases (LPMOs) have been indicated to play roles in both chitin degradation and virulence in a variety of pathogenic bacteria but are largely unexplored in this context. PubMed: 35941540DOI: 10.1186/s12866-022-02590-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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