1i35 | pdb_00001i35

SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF THE PROTEIN KINASE BYR2 FROM SCHIZOSACCHAROMYCES POMBE

spinqualitylabelsall models 1i35, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1i35 is a 1 chain structure with sequence from Schizosaccharomyces pombe. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: BYR2 (AMINO ACIDS 71 - 165) (Schizosaccharomyces pombe) Resources: FirstGlance, OCA, RCSB, PDBsum Function [BYR2_SCHPO] Serine/threonine protein kinase involved in conjugation and sporulation. It is thought that it phosphorylates the byr1 protein kinase which itself phosphorylate the spk1 kinase. Publication Abstract from PubMed BACKGROUND: After activation, small GTPases such as Ras transfer the incoming signal to effectors by specifically interacting with the binding domain of these proteins. Structural details of the binding domain of different effectors determine which pathway is predominantly activated. Byr2 from fission yeast is a functional homolog of Raf, which is the direct downstream target of Ras in mammalians that initiates a protein kinase cascade. The amino acid sequence of Byr2's Ras binding domain is only weakly related to that of Raf, and Byr2's three-dimensional structure is unknown. RESULTS: We have solved the 3D structure of the Ras binding domain of Byr2 (Byr2RBD) from Schizosaccharomyces pombe in solution. The structure consists of three alpha helices and a mixed five-stranded beta pleated sheet arranged in the topology betabetaalphabetabetaalphabetaalpha with the first seven canonic secondary structure elements forming a ubiquitin superfold. 15N-(1)H-TROSY-HSQC spectroscopy of the complex of Byr2RBD with Ras*Mg(2+)*GppNHp reveals that the first and second beta strands and the first alpha helix of Byr2 are mainly involved in the protein-protein interaction as observed in other Ras binding domains. Although the putative interaction site of H-Ras from human and Ras1 from S. pombe are identical in sequence, binding to Byr2 leads to small but significant differences in the NMR spectra, indicating a slightly different binding mode. CONCLUSIONS: The ubiquitin superfold appears to be the general structural motif for Ras binding domains even in cases with vanishing sequence identity. However, details of the 3D structure and the interacting interface are different, thereby determining the specifity of the recognition of Ras and Ras-related proteins. Solution structure of the Ras binding domain of the protein kinase Byr2 from Schizosaccharomyces pombe.,Gronwald W, Huber F, Grunewald P, Sporner M, Wohlgemuth S, Herrmann C, Kalbitzer HR Structure. 2001 Nov;9(11):1029-41. PMID:11709167 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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