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PDBsum entry 1ssc

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protein ligands Protein-protein interface(s) links
Endonuclease PDB id
1ssc
Jmol
Contents
Protein chains
112 a.a. *
11 a.a. *
Ligands
PO4
Waters ×95
* Residue conservation analysis
PDB id:
1ssc
Name: Endonuclease
Title: The 1.6 angstroms structure of a semisynthetic ribonuclease crystallized from aqueous ethanol. Comparison with crystals from salt solutions and with rnase a from aqueous alcohol solutions
Structure: Ribonuclease a. Chain: a. Engineered: yes. Ribonuclease a. Chain: b. Engineered: yes
Source: Bos taurus. Cattle. Organism_taxid: 9913. Organism_taxid: 9913
Biol. unit: Dimer (from PQS)
Resolution:
2.00Å     R-factor:   0.166    
Authors: V.S.J.De Mel,M.S.Doscher,P.D.Martin,F.Rodier,B.F.P.Edwards
Key ref:
S.J.de Mel et al. (1995). 1.6 A structure of semisynthetic ribonuclease crystallized from aqueous ethanol. Comparison with crystals from salt solutions and with ribonuclease A from aqueous alcohol solutions. Acta Crystallogr D Biol Crystallogr, 51, 1003-1012. PubMed id: 15299768 DOI: 10.1107/S0907444995004574
Date:
05-Oct-94     Release date:   26-Jan-95    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P61823  (RNAS1_BOVIN) -  Ribonuclease pancreatic
Seq:
Struc:
150 a.a.
112 a.a.
Protein chain
Pfam   ArchSchema ?
P61823  (RNAS1_BOVIN) -  Ribonuclease pancreatic
Seq:
Struc:
150 a.a.
11 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B: 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   1 term 
  Biological process     metabolic process   3 terms 
  Biochemical function     nucleic acid binding     7 terms  

 

 
DOI no: 10.1107/S0907444995004574 Acta Crystallogr D Biol Crystallogr 51:1003-1012 (1995)
PubMed id: 15299768  
 
 
1.6 A structure of semisynthetic ribonuclease crystallized from aqueous ethanol. Comparison with crystals from salt solutions and with ribonuclease A from aqueous alcohol solutions.
S.J.de Mel, M.S.Doscher, P.D.Martin, F.Rodier, B.F.Edwards.
 
  ABSTRACT  
 
The non-covalent combination of residues 1-118 of RNase A with a synthetic 14-residue peptide containing residues 111-124 of the molecule forms a highly active semisynthetic enzyme, RNase 1-118:111-124. With this enzyme, the roles played by the six C-terminal residues in generating the catalytic efficiency and substrate specificity of RNase can be studied using chemically synthesized analogs. The structure of RNase 1-118:111-124 from 43% aqueous ethanol has been determined using molecular-replacement methods and refined to a crystallographic R-factor of 0.166 for all observed reflections in the range 7.0-1.6 A (Protein Data Bank file ISSC). The structure is compared with the 2.0 A structure of RNase A from 43% aqueous 2-methyl-2-propanol and with the 1.8 A structure of the semisynthetic enzyme obtained from crystals grown in concentrated salt solution. The structure of RNase 1-118:111-124 from aqueous ethanol is virtually identical to that of RNase A from aqueous 2-methyl-2-propanol. Half of the crystallographically bound water molecules are not coincident, however. The structure is somewhat less similar to that of RNase 1-118:111-124 from salt solutions, with a major difference being the positioning of active-site residue His119.
 
  Selected figure(s)  
 
Figure 4.
Fig. 4. Electron density for Hisil9 in RNase 1-118:111-124 from aqueous ethanol. The 2F,,- F,. density peaks for the imidazole ring of Hisll9 and for the phosphate ion in RNase i-118:111-124 crystallized from aqueous ethanol contoured at 1.5cr. The side chain is in position A.
 
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1995, 51, 1003-1012) copyright 1995.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18565210 R.A.Vacca, S.Giannattasio, G.Capitani, E.Marra, and P.Christen (2008).
Molecular evolution of B6 enzymes: binding of pyridoxal-5'-phosphate and Lys41Arg substitution turn ribonuclease A into a model B6 protoenzyme.
  BMC Biochem, 9, 17.  
12486724 P.M.Tessier, H.R.Johnson, R.Pazhianur, B.W.Berger, J.L.Prentice, B.J.Bahnson, S.I.Sandler, and A.M.Lenhoff (2003).
Predictive crystallization of ribonuclease A via rapid screening of osmotic second virial coefficients.
  Proteins, 50, 303-311.  
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