1gps | pdb_00001gps

SOLUTION STRUCTURE OF GAMMA 1-H AND GAMMA 1-P THIONINS FROM BARLEY AND WHEAT ENDOSPERM DETERMINED BY 1H-NMR: A STRUCTURAL MOTIF COMMON TO TOXIC ARTHROPOD PROTEINS

spinqualitylabelsall models 1gps Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1gps is a 1 chain structure with sequence from Triticum turgidum. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 8 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DEF1_WHEAT Inhibits protein translation in cell-free systems. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The complete assignment of the proton NMR spectra of the homologous gamma 1-hordothionin and gamma 1-purothionin (47 amino acids, 4 disulfide bridges) from barley and wheat, respectively, has been performed by two-dimensional sequence-specific methods. A total of 299 proton-proton distance constraints for gamma 1-H and 285 for gamma 1-P derived from NOESY spectra have been used to calculate the three-dimensional solution structures. Initial structures have been generated by distance geometry methods and further refined by dynamical simulated annealing calculations. Both proteins show identical secondary and tertiary structure with a well-defined triple-stranded antiparallel beta-sheet (residues 1-6, 31-34, and 39-47), an alpha-helix (residues 16-28), and the corresponding connecting loops. Three disulfide bridges are located in the hydrophobic core holding together the alpha-helix and the beta-sheet and forming a cysteine-stabilized alpha-helical (CSH) motif. Moreover, a clustering of positive charges is observed on the face of the beta-sheet opposite to the helix. The three-dimensional structures of the gamma-thionins differ remarkably from plant alpha- and beta-thionins and crambin. However, they show a higher structural analogy with scorpion toxins and insect defensins which also present the CSH motif. Solution structure of gamma 1-H and gamma 1-P thionins from barley and wheat endosperm determined by 1H-NMR: a structural motif common to toxic arthropod proteins.,Bruix M, Jimenez MA, Santoro J, Gonzalez C, Colilla FJ, Mendez E, Rico M Biochemistry. 1993 Jan 19;32(2):715-24. PMID:8380707 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Plant defensin

Proteopedia Page Contributors and Editors (what is this?)

OCA