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PDBsum entry 2pkc
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Hydrolase(serine proteinase)
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PDB id
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2pkc
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Contents |
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* Residue conservation analysis
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Enzyme class:
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E.C.3.4.21.64
- peptidase K.
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Reaction:
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Hydrolysis of keratin and of other proteins, with subtilisin-like specificity. Hydrolyzes peptides amides.
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J Biol Chem
269:23108-23111
(1994)
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PubMed id:
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Crystal structure of calcium-free proteinase K at 1.5-A resolution.
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A.Müller,
W.Hinrichs,
W.M.Wolf,
W.Saenger.
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ABSTRACT
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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polypeptide backbone (i.e. no autolysis), Ca 1 has been replaced by Na+, while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.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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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.
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J Mol Model,
17,
289-300.
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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.
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Amino Acids,
37,
531-536.
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S.B.Larson,
J.S.Day,
C.Nguyen,
R.Cudney,
and
A.McPherson
(2009).
High-resolution structure of proteinase K cocrystallized with digalacturonic acid.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
65,
192-198.
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PDB code:
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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.
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BMC Struct Biol,
7,
33.
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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.
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Eur J Biochem,
269,
5536-5546.
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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.
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Eur J Biochem,
260,
752-760.
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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.
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