1ay3 | pdb_00001ay3

Nodularin from Nodularia spumigena

spinqualitylabelsall models 1ay3, 27 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ay3 is a 1 chain structure with sequence from Nodularia spumigena. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: 1ZN, ACB, FGA, MDH, MFD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The three-dimensional solution structure of nodularin was studied by NMR and molecular dynamics simulations. The conformation in water was determined from the distance and dihedral data by distance geometry and refined by iterative relaxation matrix analysis. The cyclic backbone adopts a well defined conformation but the remote parts of the side chains of arginine as well as the amino acid derivative Adda have a large spatial dispersion. For the unusual amino acids the partial charges were calculated and nodularin was subjected to molecular dynamic simulations in water. A good agreement was found between experimental and computational data with hydrogen bonds, solvent accessibility, molecular motion, and conformational exchange. The three-dimensional structure resembles very closely that of microcystin-LR in the chemically equivalent segment. Therefore, it is expected that the binding of both microcystins and nodularins to serine/threonine-specific protein phosphatases is similar on an atomic level. Solution structure of nodularin. An inhibitor of serine/threonine-specific protein phosphatases.,Annila A, Lehtimaki J, Mattila K, Eriksson JE, Sivonen K, Rantala TT, Drakenberg T J Biol Chem. 1996 Jul 12;271(28):16695-702. PMID:8663277 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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