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PDBsum entry 1ton

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protein metals links
Hydrolase(serine proteinase) PDB id
1ton
Jmol
Contents
Protein chain
228 a.a. *
Metals
_ZN
Waters ×149
* Residue conservation analysis
PDB id:
1ton
Name: Hydrolase(serine proteinase)
Title: Rat submaxillary gland serine protease, tonin. Structure sol refinement at 1.8 angstroms resolution
Structure: Tonin. Chain: a. Engineered: yes
Source: Rattus rattus. Black rat. Organism_taxid: 10117
Biol. unit: Dimer (from PQS)
Resolution:
1.80Å     R-factor:   0.196    
Authors: M.Fujinaga,M.N.G.James
Key ref: M.Fujinaga and M.N.James (1987). Rat submaxillary gland serine protease, tonin. Structure solution and refinement at 1.8 A resolution. J Mol Biol, 195, 373-396. PubMed id: 2821276
Date:
03-Jun-87     Release date:   16-Jan-88    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00759  (KLK2_RAT) -  Tonin
Seq:
Struc:
259 a.a.
228 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.21.35  - Tissue kallikrein.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa. The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg-|-Xaa bonds.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     proteolysis   1 term 
  Biochemical function     catalytic activity     6 terms  

 

 
J Mol Biol 195:373-396 (1987)
PubMed id: 2821276  
 
 
Rat submaxillary gland serine protease, tonin. Structure solution and refinement at 1.8 A resolution.
M.Fujinaga, M.N.James.
 
  ABSTRACT  
 
Tonin is a mammalian serine protease that is capable of generating the vasoconstrictive agent, angiotensin II, directly from its precursor protein, angiotensinogen, a process that normally requires two enzymes, renin and angiotensin-converting enzyme. The X-ray crystallographic structure determination and refinement of tonin at 1.8 A resolution and the analysis of the resulting model are reported. The initial phases were obtained by the method of molecular replacement using as the search model the structure of bovine trypsin. The refined model of tonin consists of 227 amino acid residues out of the 235 in the complete molecule, 149 water molecules, and one zinc ion. The R-factor (R = sigma Fo - Fc/sigma Fo) is 0.196 for the 14,997 measured data between 8 and 1.8 A resolution with I greater than or equal to sigma (I). It is estimated that the overall root-mean-square error in the coordinates is about 0.3 A. The structure of tonin that has been determined is not in its active conformation, but one that has been perturbed by the binding of Zn2+ in the active site. Zn2+ was included in the buffer to aid the crystallization. Nevertheless, the structure of tonin that is described is for the most part similar to its native form as indicated by the close tertiary structural homology with kallikrein. The differences in the structures of the two enzymes are concentrated in several loop regions; these structural differences are probably responsible for the differences in their reactivities and specificities.
 

Literature references that cite this PDB file's key reference

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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 code is shown on the right.