5aa7 | pdb_00005aa7

Structural and functional characterization of a chitin-active 15.5 kDa lytic polysaccharide monooxygenase domain from a modular chitinase from Jonesia denitrificans

spinqualitylabelsall models 5aa7, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5aa7 is a 2 chain structure with sequence from Jonesia denitrificans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.55Å Ligands: CU1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C7R4I0_JONDD Publication Abstract from PubMed Lytic polysaccharide monooxygenases (LPMOs) boost enzymatic depolymerization of recalcitrant polysaccharides, such as chitin and cellulose. We have studied a chitin-active LPMO domain (JdLPMO10A) that is considerably smaller (15.5 kDa) than all structurally characterized LPMOs so far and that is part of a modular protein containing a GH18 chitinase. The 1.55 A resolution structure revealed deletions of interacting loops that protrude from the core beta-sandwich scaffold in larger LPMO10s. Despite these deletions, the enzyme is active on alpha- and beta-chitin, and the chitin-binding surface previously described for larger LPMOs is fully conserved. JdLPMO10A may represent a minimal scaffold needed to catalyse the powerful LPMO reaction. Structural and functional characterization of a small chitin-active lytic polysaccharide monooxygenase domain of a multi-modular chitinase from Jonesia denitrificans.,Mekasha S, Forsberg Z, Dalhus B, Bacik JP, Choudhary S, Schmidt-Dannert C, Vaaje-Kolstad G, Eijsink VG FEBS Lett. 2016 Jan;590(1):34-42. doi: 10.1002/1873-3468.12025. Epub 2015 Dec 28. PMID:26763108 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chitinase 3D structures

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