1ras | pdb_00001ras

CRYSTAL STRUCTURE OF A FLUORESCENT DERIVATIVE OF RNASE A

spinqualitylabelsall models 1ras, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ras is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: AEN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RNAS1_BOVIN Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA. 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 crystal structure of RNase A chemically modified with the fluorescent probe, N-[[(iodoacetyl)-amino]ethyl]-5-naphthylamine-1-sulfonic acid (1,5-IAENS), has been solved and refined to high resolution. It yields information on the mode of binding, the mobility of a probe commonly used in spectroscopic studies, and anion binding sites in RNase A. Trigonal crystals of the fluorescent derivative grown in sodium or cesium chloride and ammonium sulfate, pH 5.1, were nearly isomorphous with those of a semisynthetic RNase [DeMel, et al. (1992) J. Biol. Chem. 267, 247-256]. Refinement starting from semisynthetic RNase led to a model with R = 20% against 1.7-A diffraction data from crystals in ammonium sulfate and another model with R = 17% against 1.9-A data taken in the presence of 3 M NaCl. The second model contains three chloride ions: one is at the active site, and the other two are at molecular interfaces. Otherwise, the two models are very similar. The fluorophore has very little effect on the protein conformation. It is found to be covalently attached to the active site His-12 with the naphthyl group stacked on the imidazole ring of His-119. It remains largely accessible to solvent and in a polar environment on the protein surface, even though the fluorescence emission spectrum is blue shifted as it is in nonpolar solvents. Crystal structure of a fluorescent derivative of RNase A.,Baudet-Nessler S, Jullien M, Crosio MP, Janin J Biochemistry. 1993 Aug 24;32(33):8457-64. PMID:8357795 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribonuclease 3D structures

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