5lpc | pdb_00005lpc

Crystal structure of Vanadium-dependent Haloperoxidase from A. marina

spinqualitylabelsall models 5lpc, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5lpc is a 1 chain structure with sequence from Acamr. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PO4 Related: 1up8 Gene: AM1_4975 (ACAMR) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Vanadium-dependent haloperoxidases (VHPOs) are an exquisite class of halogenating enzymes found in fungi, lichen, algae and bacteria. We report the cloning, purification and characterization of a functional VHPO from the cyanobacterium Acaryochloris marina (AmVHPO), including its structure determination by X-ray crystallography. The AmVHPO features a unique set of disulfide bonds, which stabilize the dodecameric assembly of the protein. Easy access by high-yield recombinant expression as well as resistance towards organic solvents and temperature, together with a distinct halogenation reactivity, make this enzyme a promising starting point for the development of biocatalytic transformations. Characterization of a Cyanobacterial Haloperoxidase and Evaluation of its Biocatalytic Halogenation Potential.,Frank A, Seel CJ, Groll M, Gulder T Chembiochem. 2016 Aug 19. doi: 10.1002/cbic.201600417. PMID:27542168 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Haloperoxidase

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