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PDBsum entry 2pkc

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protein metals links
Hydrolase(serine proteinase) PDB id
2pkc

 

 

 

 

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Contents
Protein chain
279 a.a. *
Metals
_NA
Waters ×194
* Residue conservation analysis
PDB id:
2pkc
Name: Hydrolase(serine proteinase)
Title: Crystal structure of calcium-free proteinase k at 1.5 angstroms resolution
Structure: Proteinase k. Chain: a. Engineered: yes
Source: Engyodontium album. Organism_taxid: 37998
Resolution:
1.50Å     R-factor:   0.201    
Authors: A.Mueller,W.Hinrichs,W.M.Wolf,W.Saenger
Key ref: A.Müller et al. (1994). Crystal structure of calcium-free proteinase K at 1.5-A resolution. J Biol Chem, 269, 23108-23111. PubMed id: 8083213
Date:
04-Jun-93     Release date:   31-Jan-94    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P06873  (PRTK_PARAQ) -  Proteinase K from Parengyodontium album
Seq:
Struc:
384 a.a.
279 a.a.
Key:    PfamA domain  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 269:23108-23111 (1994)
PubMed id: 8083213  
 
 
Crystal structure of calcium-free proteinase K at 1.5-A resolution.
A.Müller, W.Hinrichs, W.M.Wolf, W.Saenger.
 
  ABSTRACT  
 
Proteinase K from the fungus Tritirachium album Limber binds two Ca2+ ions, one strongly (Ca 1) and the other weakly (Ca 2). Removal of these cations reduces the stability of proteinase K as shown by thermal denaturation, but the proteolytic activity is unchanged. The x-ray structures of native and Ca(2+)-free proteinase K at 1.5-A resolution show that there are no cuts in the polypeptide backbone (i.e. no autolysis), Ca 1 has been replaced by Na+, while Ca 2 has been substituted by a water associated with a larger but locally confined structural change at that site. A small but concerted geometrical shift is transmitted from the Ca 1 site via eight secondary structure elements to the substrate recognition site (Gly100-Tyr104, and Ser132-Gly136) but not to the catalytic triad (Asp39,His69,Ser224). This is accompanied by positional changes of localized waters.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20446009 S.Q.Liu, Y.Tao, Z.H.Meng, Y.X.Fu, and K.Q.Zhang (2011).
The effect of calciums on molecular motions of proteinase K.
  J Mol Model, 17, 289-300.  
19326044 N.Hovhannisyan, S.h.Harutyunyan, A.Hovhannisyan, A.Hambardzumyan, M.Chitchyan, M.Melkumyan, G.Oganezova, and N.Avetisyan (2009).
The novel inhibitors of serine proteases.
  Amino Acids, 37, 531-536.  
  19255463 S.B.Larson, J.S.Day, C.Nguyen, R.Cudney, and A.McPherson (2009).
High-resolution structure of proteinase K cocrystallized with digalacturonic acid.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 192-198.
PDB code: 3dyb
17511867 S.Q.Liu, Z.H.Meng, J.K.Yang, Y.X.Fu, and K.Q.Zhang (2007).
Characterizing structural features of cuticle-degrading proteases from fungi by molecular modeling.
  BMC Struct Biol, 7, 33.  
12423352 J.Arnórsdottir, R.B.Smáradóttir, O.T.Magnússon, S.H.Thorbjarnardóttir, G.Eggertsson, and M.M.Kristjánsson (2002).
Characterization of a cloned subtilisin-like serine proteinase from a psychrotrophic Vibrio species.
  Eur J Biochem, 269, 5536-5546.  
10103004 M.M.Kristjánsson, O.T.Magnússon, H.M.Gudmundsson, G.A.Alfredsson, and H.Matsuzawa (1999).
Properties of a subtilisin-like proteinase from a psychrotrophic Vibrio species comparison with proteinase K and aqualysin I.
  Eur J Biochem, 260, 752-760.  
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.

 

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