PDBsum entry 4n4c

Hydrolase

PDB id: 4n4c

Contents

Protein chains

124 a.a.

Ligands

PO4 ×2

Waters ×35

PDB id:

4n4c

Name:

Hydrolase

Title:

Crystal structure of thE C-terminal swapped dimer of a bovine seminal ribonuclease mutant

Structure:

Seminal ribonuclease. Chain: a, b. Fragment: unp residues 27-150. Synonym: s-rnase, seminal rnase, ribonuclease bs-1. Engineered: yes. Mutation: yes

Source:

Bos taurus. Bovine,cow,domestic cattle,domestic cow. Organism_taxid: 9913. Gene: srn. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.48Å R-factor: 0.171 R-free: 0.186

Authors:

A.Pica,I.Russo Krauss,A.Merlino,F.Sica

Key ref:

F.Sica et al. (2013). The multiple forms of bovine seminal ribonuclease: structure and stability of a C-terminal swapped dimer. Febs Lett, 587, 3755-3762. PubMed id: 24140346 DOI: 10.1016/j.febslet.2013.10.003

Date:

08-Oct-13 Release date: 06-Nov-13

Protein chains

P00669  (RNS_BOVIN) -  Seminal ribonuclease from Bos taurus

Seq: 150 a.a.

Struc: 124 a.a.*

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.4.6.1.18 - pancreatic ribonuclease.
• Reaction:
  1. an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine- 3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA]
  2. an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA]

DOI no: 10.1016/j.febslet.2013.10.003

Febs Lett 587:3755-3762 (2013)

PubMed id: 24140346

The multiple forms of bovine seminal ribonuclease: structure and stability of a C-terminal swapped dimer.

F.Sica, A.Pica, A.Merlino, I.Russo Krauss, C.Ercole, D.Picone.

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.