4N4C

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

Summary for 4N4C

• Entry DOI: 10.2210/pdb4n4c/pdb
• Related: 1F0V 1N1X 3RID
• Descriptor: Seminal ribonuclease, PHOSPHATE ION (3 entities in total)
• Functional Keywords: c-terminal domain swapping, hydrolase, ribonuclease
• Biological source: Bos taurus (bovine,cow,domestic cattle,domestic cow)
• Cellular location: Secreted: P00669
• Total number of polymer chains: 2
• Total formula weight: 27633.41

Authors

Pica, A.,Russo Krauss, I.,Merlino, A.,Sica, F. (deposition date: 2013-10-08, release date: 2013-11-06, Last modification date: 2023-09-20)

Primary citation

Sica, F.,Pica, A.,Merlino, A.,Russo Krauss, I.,Ercole, C.,Picone, D.
The multiple forms of bovine seminal ribonuclease: Structure and stability of a C-terminal swapped dimer.
Febs Lett., 587:3755-3762, 2013

PubMed Abstract: Bovine seminal ribonuclease (BS-RNase) acquires an interesting anti-tumor activity associated with the swapping on the N-terminal. 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.

PubMed: 24140346
DOI: 10.1016/j.febslet.2013.10.003

Experimental method

X-RAY DIFFRACTION (2.48 Å)