4n4c

Crystal structure of the C-terminal swapped dimer of a Bovine seminal ribonuclease mutant

spinqualitylabelsall models 4n4c, resolution 2.48Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4n4c 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 2.48Å Ligands: PO4, YCM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RNS_BOVIN This enzyme hydrolyzes both single- and double-stranded RNA. Publication Abstract from PubMed Bovine seminal ribonuclease (BS-RNase) acquires an interesting anti-tumor activity associated with the swapping on the N-termini. The first direct experimental evidence on the formation of a C-terminal swapped dimer (C-dimer) obtained from the monomeric derivative of BS-RNase, although under non-native conditions, is here reported. The X-ray model of this dimer reveals a quaternary structure different from that of the C-dimer of RNase A, due to the presence of three mutations in the hinge peptide 111-116. The mutations increase the hinge peptide flexibility and decrease the stability of the C-dimer against dissociation. The biological implications of the structural data are also discussed. The multiple forms of Bovine Seminal Ribonuclease: structure and stability of a C-terminal swapped dimer.,Sica F, Pica A, Merlino A, Krauss IR, Ercole C, Picone D FEBS Lett. 2013 Oct 15. pii: S0014-5793(13)00745-X. doi:, 10.1016/j.febslet.2013.10.003. PMID:24140346 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribonuclease 3D structures

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