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PDBsum entry 3tsr

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protein ligands Protein-protein interface(s) links
Hydrolase/hydrolase inhibitor PDB id
3tsr
Jmol PyMol
Contents
Protein chains
124 a.a.
117 a.a.
457 a.a.
Ligands
EDO ×13
PEG
Waters ×822
PDB id:
3tsr
Name: Hydrolase/hydrolase inhibitor
Title: X-ray structure of mouse ribonuclease inhibitor complexed wi ribonuclease 1
Structure: Ribonuclease pancreatic. Chain: a, b, c, d. Synonym: rnase 1, rnase a. Engineered: yes. Ribonuclease inhibitor. Chain: e, f, g, h. Synonym: ribonuclease/angiogenin inhibitor 1. Engineered: yes
Source: Mus musculus. Mouse. Organism_taxid: 10090. Strain: c57bl/6j. Gene: rib-1, rib1, rnase1, rns1. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: rnh, rnh1.
Resolution:
2.20Å     R-factor:   0.183     R-free:   0.233
Authors: A.Chang,J.E.Lomax,C.A.Bingman,R.T.Raines,G.N.Phillips Jr.
Key ref: J.E.Lomax et al. (2014). Functional evolution of ribonuclease inhibitor: insights from birds and reptiles. J Mol Biol, 426, 3041-3056. PubMed id: 24941155 DOI: 10.1016/j.jmb.2014.06.007
Date:
13-Sep-11     Release date:   19-Sep-12    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00683  (RNAS1_MOUSE) -  Ribonuclease pancreatic
Seq:
Struc:
149 a.a.
124 a.a.
Protein chains
Pfam   ArchSchema ?
P00683  (RNAS1_MOUSE) -  Ribonuclease pancreatic
Seq:
Struc:
149 a.a.
117 a.a.
Protein chains
Pfam   ArchSchema ?
Q91VI7  (RINI_MOUSE) -  Ribonuclease inhibitor
Seq:
Struc:
456 a.a.
457 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D: 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.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   6 terms 
  Biological process     nucleic acid phosphodiester bond hydrolysis   5 terms 
  Biochemical function     nucleic acid binding     7 terms  

 

 
DOI no: 10.1016/j.jmb.2014.06.007 J Mol Biol 426:3041-3056 (2014)
PubMed id: 24941155  
 
 
Functional evolution of ribonuclease inhibitor: insights from birds and reptiles.
J.E.Lomax, C.M.Bianchetti, A.Chang, G.N.Phillips, B.G.Fox, R.T.Raines.
 
  ABSTRACT  
 
Ribonuclease inhibitor (RI) is a conserved protein of the mammalian cytosol. RI binds with high affinity to diverse secretory ribonucleases (RNases) and inhibits their enzymatic activity. Although secretory RNases are found in all vertebrates, the existence of a non-mammalian RI has been uncertain. Here, we report on the identification and characterization of RI homologs from chicken and anole lizard. These proteins bind to RNases from multiple species but exhibit much greater affinity for their cognate RNases than for mammalian RNases. To reveal the basis for this differential affinity, we determined the crystal structure of mouse, bovine, and chicken RI·RNase complexes to a resolution of 2.20, 2.21, and 1.92Å, respectively. A combination of structural, computational, and bioinformatic analyses enabled the identification of two residues that appear to contribute to the differential affinity for RNases. We also found marked differences in oxidative instability between mammalian and non-mammalian RIs, indicating evolution toward greater oxygen sensitivity in RIs from mammalian species. Taken together, our results illuminate the structural and functional evolution of RI, along with its dynamic role in vertebrate biology.
 

 

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