8cc5 | pdb_00008cc5

Vibrio cholerae GbpA (LPMO domain)

spinqualitylabelsall models 8cc5, resolution 1.62Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8cc5 is a 2 chain structure with sequence from Vibrio cholerae O1 biovar El Tor. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.62Å Ligands: ACT, CU, NA, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A6XA54_VIBCE Probably interacts with GlcNAc residues. May promote attachment to both epithelial cell surfaces and chitin.[HAMAP-Rule:MF_01905] Publication Abstract from PubMed Lytic polysaccharide monooxygenases (LPMOs) are surface-active redox enzymes that catalyze the degradation of recalcitrant polysaccharides, making them important tools for energy production from renewable sources. In addition, LPMOs are important virulence factors for fungi, bacteria, and viruses. However, many knowledge gaps still exist regarding their catalytic mechanism and interaction with their insoluble, crystalline substrates. Moreover, conventional structural biology techniques, such as X-ray crystallography, usually do not reveal the protonation state of catalytically important residues. In contrast, neutron crystallography is highly suited to obtain this information, albeit with significant sample volume requirements and challenges associated with hydrogen's large incoherent scattering signal. We set out to demonstrate the feasibility of neutron-based techniques for LPMOs using N-acetylglucosamine-binding protein A (GbpA) from Vibrio cholerae as a target. GbpA is a multifunctional protein that is secreted by the bacteria to colonize and degrade chitin. We developed an efficient deuteration protocol, which yields >10 mg of pure 97% deuterated protein per liter expression media, which was scaled up further at international facilities. The deuterated protein retains its catalytic activity and structure, as demonstrated by small-angle X-ray and neutron scattering studies of full-length GbpA and X-ray crystal structures of its LPMO domain (to 1.1 A resolution), setting the stage for neutron scattering experiments with its substrate chitin. Perdeuterated GbpA Enables Neutron Scattering Experiments of a Lytic Polysaccharide Monooxygenase.,Sorensen HV, Montserrat-Canals M, Loose JSM, Fisher SZ, Moulin M, Blakeley MP, Cordara G, Bjerregaard-Andersen K, Krengel U ACS Omega. 2023 Jul 31;8(32):29101-29112. doi: 10.1021/acsomega.3c02168. , eCollection 2023 Aug 15. PMID:37599915 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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