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PDBsum entry 1fon
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Serine protease
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PDB id
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1fon
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Serine protease
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Title:
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Crystal structure of bovine procarboxypeptidase a-s6 subunit iii, a highly structured truncated zymogen e
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Structure:
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Procarboxypeptidase a-s6. Chain: a, b. Fragment: subunit iii. Synonym: bovine subunit iii
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Source:
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Bos taurus. Cattle. Organism_taxid: 9913. Organ: pancreas
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Biol. unit:
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Dimer (from
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Resolution:
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1.70Å
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R-factor:
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0.184
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R-free:
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0.220
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Authors:
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D.C.Pignol,T.Gaboriaud,B.Michon,B.Kerfelec,C.Chapus,J.C.Fontecilla- Camps
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Key ref:
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D.Pignol
et al.
(1994).
Crystal structure of bovine procarboxypeptidase A-S6 subunit III, a highly structured truncated zymogen E.
Embo J,
13,
1763-1771.
PubMed id:
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Date:
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01-Feb-96
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Release date:
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14-Oct-96
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PROCHECK
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Headers
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References
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P05805
(CAC3_BOVIN) -
Proproteinase E from Bos taurus
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Seq:
Struc:
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253 a.a.
232 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Embo J
13:1763-1771
(1994)
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PubMed id:
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Crystal structure of bovine procarboxypeptidase A-S6 subunit III, a highly structured truncated zymogen E.
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D.Pignol,
C.Gaboriaud,
T.Michon,
B.Kerfelec,
C.Chapus,
J.C.Fontecilla-Camps.
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ABSTRACT
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Subunit III, a defective serine endopeptidase lacking the typical N-terminal
hydrophobic dipeptide is secreted by the pancreas of ruminant species as part of
the bovine ternary complex procarboxypeptidase A-S6. Two monoclinic crystal
forms were obtained and subsequently used to solve its X-ray structure. The
highest resolution model of subunit III was refined at 1.7 A resolution to a
crystallographic R-factor of 18.4%, with r.m.s. bond deviations from ideality of
0.012 A. About 80% of the model presents the characteristic architecture of
trypsin-like proteases. The remaining zones, however, have well-defined, unique
conformations. The regions from residues 70 to 80 and from 140 to 155 present
maximum distances of 16 and 18 A relative to serine proteases and zymogens.
Comparisons with the structures of porcine elastase 1 and chymotrypsinogen A
indicate that the specific binding pocket of subunit III adopts a zymogen-like
conformation and thus provide a basis for its inactivity. In general, the
structural analysis of subunit III strongly suggests that it corresponds to a
truncated version of a new class of highly structured elastase-like zymogen
molecules. Based on the structures of subunit III and elastase 1, it is
concluded that large concerted movements are necessary for the activation of
zymogen E.
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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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P.Gál,
V.Harmat,
A.Kocsis,
T.Bián,
L.Barna,
G.Ambrus,
B.Végh,
J.Balczer,
R.B.Sim,
G.Náray-Szabó,
and
P.Závodszky
(2005).
A true autoactivating enzyme. Structural insight into mannose-binding lectin-associated serine protease-2 activations.
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J Biol Chem,
280,
33435-33444.
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PDB code:
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C.P.Sommerhoff,
W.Bode,
P.J.Pereira,
M.T.Stubbs,
J.Stürzebecher,
G.P.Piechottka,
G.Matschiner,
and
A.Bergner
(1999).
The structure of the human betaII-tryptase tetramer: fo(u)r better or worse.
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Proc Natl Acad Sci U S A,
96,
10984-10991.
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H.Jing,
K.J.Macon,
D.Moore,
L.J.DeLucas,
J.E.Volanakis,
and
S.V.Narayana
(1999).
Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D.
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EMBO J,
18,
804-814.
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PDB code:
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F.X.Gomis-Rüth,
M.Gómez,
W.Bode,
R.Huber,
and
F.X.Avilés
(1995).
The three-dimensional structure of the native ternary complex of bovine pancreatic procarboxypeptidase A with proproteinase E and chymotrypsinogen C.
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EMBO J,
14,
4387-4394.
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PDB code:
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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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Links
