3fl1 | pdb_00003fl1

X-ray structure of the non covalent swapped form of the A19P/Q28L/K31C/S32C mutant of bovine pancreatic ribonuclease in complex with 2'-DEOXYCYTIDINE-2'-DEOXYGUANOSINE-3',5'-MONOPHOSPHATE

spinqualitylabelsall models 3fl1, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3fl1 is a 2 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 1.9Å Ligands: CGP, GLC, PRD_900006, SO4, YCM 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 cytotoxic action of bovine seminal ribonuclease (BS-RNase) depends on its non-covalent swapped dimeric form (NCD-BS), which presents a compact structure that allows the molecule to escape ribonuclease inhibitor (RI). A key role in the acquisition of this structure has been attributed to the concomitant presence of a proline in position 19 and a leucine in position 28. The introduction of Leu28, Cys31 and Cys32 and, in addition, of Pro19 in the sequence of bovine pancreatic ribonuclease (RNase A) has produced two dimeric variants LCC and PLCC, which do exhibit a cytotoxic activity, though at a much lower level than BS-RNase. The crystal structure analysis of the non-covalent swapped form (NCD) of LCC and PLCC, complexed with the substrate analogue 2'-deoxycytidylyl(3',5')-2'-deoxyguanosine, has revealed that, differently from NCD-BS, the dimers adopt an opened quaternary structure, with the two Leu residues fully exposed to the solvent, that does not hinder the binding of RI. Similar results have been obtained for a third mutant of the pancreatic enzyme, engineered with the hinge peptide sequence of the seminal enzyme (residues 16-22) and the two cysteines in position 31 and 32, but lacking the hydrophobic Leu residue in position 28. The comparison of these three structures with those previously reported for other ribonuclease swapped dimers strongly suggests that, in addition to Pro19 and Leu28, the presence of a glycine at the N-terminal end of the hinge peptide is also important to push the swapped form of RNase A dimer into the compact quaternary organization observed for NCD-BS. (c) 2009 Wiley Periodicals, Inc. Biopolymers, 2009. Towards an antitumor form of bovine pancreatic ribonuclease: The crystal structure of three non-covalent dimeric mutants.,Merlino A, Krauss IR, Perillo M, Mattia CA, Ercole C, Picone D, Vergara A, Sica F Biopolymers. 2009 Mar 11. PMID:19280639 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribonuclease 3D structures

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