6fpd

AB21 protein from Agaricus bisporus

spinqualitylabelsall models 6fpd, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6fpd is a 1 chain structure with sequence from Agaricus bisporus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: EDO, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A384E160_AGABI Publication Abstract from PubMed We report the characterization of the dimeric protein AB21 from Agaricus bisporus, one of the most commonly and widely consumed mushrooms in the world. The protein shares no significant sequence similarity with any protein of known function, and it is the first characterized member of its protein family. The coding sequence of the ab21 gene was determined and the protein was expressed in E. coli in a recombinant form. We demonstrated a high thermal and pH stability of AB21 and proved the weak affinity of the protein to divalent ions of some transition metals (nickel, zinc, cadmium and cobalt). The reported crystallographic structure exhibits an interesting rod-like helical bundle fold with structural similarity to bacterial toxins of the ClyA superfamily. By immunostaining, we demonstrated an abundance of AB21 in the fruiting bodies of A. bisporus. This article is protected by copyright. All rights reserved. Structure and properties of AB21, a novel A. bisporus protein with structural relation to bacterial pore-forming toxins.,Komarek J, Ivanov Kavkova E, Houser J, Horackova A, Zdanska J, Demo G, Wimmerova M Proteins. 2018 May 2. doi: 10.1002/prot.25522. PMID:29722060 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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