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PDBsum entry 1p3c
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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Glutamyl endopeptidase from bacillus intermedius
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Structure:
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Glutamyl-endopeptidase. Chain: a
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Source:
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Bacillus intermedius. Organism_taxid: 1400. Strain: 3-19
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Biol. unit:
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Dimer (from
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Resolution:
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1.50Å
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R-factor:
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0.156
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R-free:
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0.184
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Authors:
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R.Meijers,E.V.Blagova,V.M.Levdikov,G.N.Rudenskaya,G.G.Chestukhina, T.V.Akimkina,S.V.Kostrov,V.S.Lamzin,I.P.Kuranova
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Key ref:
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R.Meijers
et al.
(2004).
The crystal structure of glutamyl endopeptidase from Bacillus intermedius reveals a structural link between zymogen activation and charge compensation.
Biochemistry,
43,
2784-2791.
PubMed id:
DOI:
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Date:
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17-Apr-03
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Release date:
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27-Apr-04
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PROCHECK
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Headers
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References
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Q9EXR9
(Q9EXR9_BACIN) -
Serine protease from Bacillus intermedius
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Seq:
Struc:
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303 a.a.
215 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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DOI no:
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Biochemistry
43:2784-2791
(2004)
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PubMed id:
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The crystal structure of glutamyl endopeptidase from Bacillus intermedius reveals a structural link between zymogen activation and charge compensation.
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R.Meijers,
E.V.Blagova,
V.M.Levdikov,
G.N.Rudenskaya,
G.G.Chestukhina,
T.V.Akimkina,
S.V.Kostrov,
V.S.Lamzin,
I.P.Kuranova.
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ABSTRACT
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Extracellular glutamyl endopeptidase from Bacillus intermedius (BIEP) is a
chymotrypsin-like serine protease which cleaves the peptide bond on the carboxyl
side of glutamic acid. Its three-dimensional structure was determined for
C222(1) and C2 crystal forms of BIEP to 1.5 and 1.75 A resolution, respectively.
The topology of BIEP diverges from the most common chymotrypsin architecture,
because one of the domains consists of a beta-sandwich consisting of two
antiparallel beta-sheets and two helices. In the C2 crystals, a
2-methyl-2,4-pentanediol (MPD) molecule was found in the substrate binding site,
mimicking a glutamic acid. This enabled the identification of the residues
involved in the substrate recognition. The presence of the MPD molecule causes a
change in the active site; the interaction between two catalytic residues (His47
and Ser171) is disrupted. The N-terminal end of the enzyme is involved in the
formation of the substrate binding pocket. This indicates a direct relation
between zymogen activation and substrate charge compensation.
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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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T.K.Nemoto,
T.Ono,
Y.Shimoyama,
S.Kimura,
and
Y.Ohara-Nemoto
(2009).
Determination of three amino acids causing alteration of proteolytic activities of staphylococcal glutamyl endopeptidases.
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Biol Chem,
390,
277-285.
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E.V.Gasanov,
I.V.Demidyuk,
A.V.Shubin,
V.I.Kozlovskiy,
O.G.Leonova,
and
S.V.Kostrov
(2008).
Hetero- and auto-activation of recombinant glutamyl endopeptidase from Bacillus intermedius.
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Protein Eng Des Sel,
21,
653-658.
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N.S.Velishaeva,
E.V.Gasanov,
T.Y.Gromova,
and
I.V.Demidyuk
(2008).
[Effect of a Modification of the Processing Site of Bacillus intermedius Glutamyl Endopeptidase on the Production of Active Enzyme by Bacillus subtilis Cells.]
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Bioorg Khim,
34,
786-791.
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N.Yang,
J.Nan,
E.Brostromer,
R.Hatti-Kaul,
and
X.D.Su
(2008).
Crystal structure of an alkaline serine protease from Nesterenkonia sp. defines a novel family of secreted bacterial proteases.
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Proteins,
73,
1072-1075.
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PDB code:
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M.R.Sharipova,
E.I.Shagimardanova,
I.B.Chastukhina,
T.R.Shamsutdinov,
N.P.Balaban,
A.M.Mardanova,
G.N.Rudenskaya,
I.V.Demidyuk,
and
S.V.Kostrov
(2007).
The expression of Bacillus intermedius glutamyl endopeptidase gene in Bacillus subtilis recombinant strains.
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Mol Biol Rep,
34,
79-87.
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J.R.Birtley,
S.R.Knox,
A.M.Jaulent,
P.Brick,
R.J.Leatherbarrow,
and
S.Curry
(2005).
Crystal structure of foot-and-mouth disease virus 3C protease. New insights into catalytic mechanism and cleavage specificity.
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J Biol Chem,
280,
11520-11527.
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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
