 |
PDBsum entry 2pkc
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Hydrolase(serine proteinase)
|
PDB id
|
|
|
|
2pkc
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal structure of calcium-Free proteinase k at 1.5-A resolution.
|
|
|
Authors
|
|
A.Müller,
W.Hinrichs,
W.M.Wolf,
W.Saenger.
|
|
|
Ref.
|
|
J Biol Chem, 1994,
269,
23108-23111.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
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polypeptide backbone (i.e. no autolysis), Ca 1 has been replaced by Na+, while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.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Long-Range structural changes in proteinase k triggered by calcium ion removal.
|
|
|
Authors
|
|
J.Bajorath,
S.Raghunathan,
W.Hinrichs,
W.Saenger.
|
|
|
Ref.
|
|
Nature, 1989,
337,
481-484.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #2
|
|
|
Title
|
|
Three-Dimensional structure of proteinase k at 0.15-Nm resolution.
|
|
|
Authors
|
|
C.Betzel,
G.P.Pal,
W.Saenger.
|
|
|
Ref.
|
|
Eur J Biochem, 1988,
178,
155-171.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
