6t5z

Crystal structure of an AA10 LPMO from Photorhabdus luminescens

spinqualitylabelsall models 6t5z, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6t5z is a 3 chain structure with sequence from Photorhabdus laumondii subsp. laumondii TTO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6000031Å Ligands: CU Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q7N4I5_PHOLL Publication Abstract from PubMed Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes involved in the degradation of recalcitrant polysaccharides such as cellulose or chitin. LPMOs act in synergy with glycoside hydrolases such as cellulases and chitinases by oxidatively cleaving a number of glycosidic bonds at the surface of their crystalline substrate(s). Besides their role in biomass degradation, some bacterial LPMOs have been found to be virulence factors in some human and insect pathogens. Photorhabdus luminescens is a nematode symbiont bacterium that is pathogenic to a wide range of insects. A single gene encoding a LPMO is found in its genome. In this work, we report the characterization of this LPMO, referred to as PlAA10. Surprisingly, PlAA10 lacks the conserved alanine residue (substituted by an isoleucine) found in the second coordination sphere of the copper active site in bacterial LPMOs. PlAA10 was found to be catalytically active on both alpha- and beta-chitin, and exhibits a C1-oxidation regiospecificity, similarly to other chitin-active LPMOs. The 1.6 A X-ray crystal structure confirmed that PlAA10 adopts the canonical immunoglobulin-like fold typical for LPMOs. The geometry of the copper active site is not affected by the nearby isoleucine, as also supported by electron paramagnetic resonance. Nevertheless, the bulkier side chain of isoleucine protrudes from the substrate-binding surface. A bioinformatic study on putative bacterial LPMOs unveiled that they exhibit some variability at the conserved active site alanine position with a substitution in about 15% of all sequences analyzed. Characterization of a bacterial copper-dependent lytic polysaccharide monooxygenase with an unusual second coordination sphere.,Munzone A, El Kerdi B, Fanuel M, Rogniaux H, Ropartz D, Reglier M, Royant A, Simaan AJ, Decroos C FEBS J. 2020 Jan 5. doi: 10.1111/febs.15203. PMID:31903721 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Monooxygenase 3D structures

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