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PDBsum entry 1o0g

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protein links
Hydrolase PDB id
1o0g
Jmol
Contents
Protein chain
124 a.a.
Superseded by: 1qwq
PDB id:
1o0g
Name: Hydrolase
Title: Solution structure of the monomeric n67d mutant of bovine seminal ribonuclease
Structure: Ribonuclease. Chain: a. Synonym: seminal ribonuclease. Engineered: yes. Mutation: yes
Source: Bos taurus. Bovine. Expressed in: escherichia coli.
NMR struc: 16 models
Authors: F.Avitabile,C.Alfano,R.Spadaccini,O.Crescenzi,A.M.D'Ursi, G.D'Alessio,T.Tancredi,D.Picone
Key ref:
F.Avitabile et al. (2003). The swapping of terminal arms in ribonucleases: comparison of the solution structure of monomeric bovine seminal and pancreatic ribonucleases. Biochemistry, 42, 8704-8711. PubMed id: 12873130 DOI: 10.1021/bi0342517
Date:
21-Feb-03     Release date:   15-Jul-03    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00669  (RNS_BOVIN) -  Seminal ribonuclease
Seq:
Struc:
150 a.a.
124 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.1.27.5  - Pancreatic ribonuclease.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in C-P or U-P with 2',3'-cyclic phosphate intermediates.

 

 
DOI no: 10.1021/bi0342517 Biochemistry 42:8704-8711 (2003)
PubMed id: 12873130  
 
 
The swapping of terminal arms in ribonucleases: comparison of the solution structure of monomeric bovine seminal and pancreatic ribonucleases.
F.Avitabile, C.Alfano, R.Spadaccini, O.Crescenzi, A.M.D'Ursi, G.D'Alessio, T.Tancredi, D.Picone.
 
  ABSTRACT  
 
Bovine seminal ribonuclease (BS-RNase), the only dimeric protein among the pancreatic-like ribonucleases, is endowed with special structural features and with biological functions beyond enzymatic activity. In solution, the protein exists as an equilibrium mixture of two forms, with or without exchange (or swapping) of the N-terminal arms. After selective reduction and alkylation of the two intrachain disulfide bridges, the dimeric protein can be transformed into a monomeric derivative that has a ribonuclease activity higher than that of the parent dimeric protein but is devoid of the special biological functions. A detailed investigation of the structural features of this protein in solution, in comparison with those of other monomeric ribonucleases, may help unveil the structural details which induce swapping of the N-terminal arms of BS-RNase. The solution structure of the recombinant monomeric form of BS-RNase, as determined by 3D heteronuclear NMR, shows close similarity with that of bovine pancreatic ribonuclease (RNase A) in all regions characterized by regular elements of secondary structure. However, significant differences are present in the flexible regions, which could account for the different behavior of the two proteins. To characterize in detail these regions, we have measured H/D exchange rate constants, temperature coefficients and heteronuclear NOEs of backbone amides for both RNase A and monomeric BS-RNase. The results indicate a large difference in the backbone flexibility of the hinge peptide segment 16-22 of the two proteins, which could provide the molecular basis to explain the ability of BS-RNase subunits to swap their N-terminal arms.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21122069 C.Giancola, C.Ercole, I.Fotticchia, R.Spadaccini, E.Pizzo, G.D'Alessio, and D.Picone (2011).
Structure-cytotoxicity relationships in bovine seminal ribonuclease: new insights from heat and chemical denaturation studies on variants.
  FEBS J, 278, 111-122.  
19263489 C.Ercole, R.A.Colamarino, E.Pizzo, F.Fogolari, R.Spadaccini, and D.Picone (2009).
Comparison of the structural and functional properties of RNase A and BS-RNase: A stepwise mutagenesis approach.
  Biopolymers, 91, 1009-1017.  
16519682 M.Rodríguez, A.Benito, M.Ribó, and M.Vilanova (2006).
Characterization of the dimerization process of a domain-swapped dimeric variant of human pancreatic ribonuclease.
  FEBS J, 273, 1166-1176.  
15647261 D.Picone, A.Di Fiore, C.Ercole, M.Franzese, F.Sica, S.Tomaselli, and L.Mazzarella (2005).
The role of the hinge loop in domain swapping. The special case of bovine seminal ribonuclease.
  J Biol Chem, 280, 13771-13778.
PDB codes: 1y92 1y94
15192098 F.Sica, A.Di Fiore, A.Merlino, and L.Mazzarella (2004).
Structure and stability of the non-covalent swapped dimer of bovine seminal ribonuclease: an enzyme tailored to evade ribonuclease protein inhibitor.
  J Biol Chem, 279, 36753-36760.
PDB code: 1tq9
14622261 C.Ercole, F.Avitabile, P.Del Vecchio, O.Crescenzi, T.Tancredi, and D.Picone (2003).
Role of the hinge peptide and the intersubunit interface in the swapping of N-termini in dimeric bovine seminal RNase.
  Eur J Biochem, 270, 4729-4735.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.