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PDBsum entry 1ptk

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protein metals links
Hydrolase(serine proteinase) PDB id
1ptk

 

 

 

 

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Contents
Protein chain
279 a.a. *
Metals
_HG ×2
_CA
Waters ×198
* Residue conservation analysis
PDB id:
1ptk
Name: Hydrolase(serine proteinase)
Title: Studies on the inhibitory action of mercury upon proteinase k
Structure: Proteinase k. Chain: a. Engineered: yes
Source: Engyodontium album. Organism_taxid: 37998
Resolution:
2.40Å     R-factor:   0.126    
Authors: A.Mueller,W.Saenger
Key ref: A.Müller and W.Saenger (1993). Studies on the inhibitory action of mercury upon proteinase K. J Biol Chem, 268, 26150-26154. PubMed id: 8253733
Date:
07-Apr-93     Release date:   31-Jan-94    
PROCHECK
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 Headers
 References

Protein chain
P06873  (PRTK_PARAQ) -  Proteinase K from Parengyodontium album
Seq:
Struc:
384 a.a.
279 a.a.
Key:    Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.21.64  - peptidase K.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of keratin and of other proteins, with subtilisin-like specificity. Hydrolyzes peptides amides.

 

 
J Biol Chem 268:26150-26154 (1993)
PubMed id: 8253733  
 
 
Studies on the inhibitory action of mercury upon proteinase K.
A.Müller, W.Saenger.
 
  ABSTRACT  
 
In proteinase K, Cys73 is located "below" the imidazole of the active site His69. In a 2.4-A resolution x-ray crystal structure of the complex formed between the enzyme and HgAc2, two Hg(II) positions are found: a fully occupied site, covalently bound to Cys73 (S gamma), which disrupts the catalytic triad (Asp39-His69-Ser224), and a 2-fold disordered (25 and 35% occupancy), noncovalent complexation to His72, Cys73, and Thr76 of lower affinity. The enzyme is inhibited noncompetitively at low concentrations and competitively above stoichiometric concentrations of Hg(II), but it retains 7% residual activity. This can be rationalized if the molecule is flexible enough to permit transient formation of the catalytic triad. Except for the active site, only minor structural changes are observed upon binding of Hg(II), but the thermal stability is reduced by 4 degrees C.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20490658 J.J.Panek, R.Mazzarello, M.Novič, and A.Jezierska-Mazzarello (2011).
Impact of Mercury(II) on proteinase K catalytic center: investigations via classical and Born-Oppenheimer molecular dynamics.
  Mol Divers, 15, 215-226.  
19530137 C.D.Matheson, T.E.Marion, S.Hayter, N.Esau, R.Fratpietro, and K.K.Vernon (2009).
Technical note: removal of metal ion inhibition encountered during DNA extraction and amplification of copper-preserved archaeological bone using size exclusion chromatography.
  Am J Phys Anthropol, 140, 384-391.  
18367466 M.D.Rand, C.E.Bland, and J.Bond (2008).
Methylmercury activates enhancer-of-split and bearded complex genes independent of the notch receptor.
  Toxicol Sci, 104, 163-176.  
17309445 E.K.Kotlova, N.M.Ivanova, M.P.Yusupova, T.L.Voyushina, N.E.Ivanushkina, and G.G.Chestukhina (2007).
Thiol-dependent serine proteinase from Paecilomyces lilacinus: purification and catalytic properties.
  Biochemistry (Mosc), 72, 117-123.  
15330798 F.Lewis, P.Jackson, S.Lane, G.Coast, and A.M.Hanby (2004).
Testing for HER2 in breast cancer.
  Histopathology, 45, 207-217.  
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.

 

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