 |
PDBsum entry 1p3c
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
The crystal structure of glutamyl endopeptidase from bacillus intermedius reveals a structural link between zymogen activation and charge compensation.
|
|
|
Authors
|
|
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.
|
|
|
Ref.
|
|
Biochemistry, 2004,
43,
2784-2791.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
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.
|
|
|
|
|
|
|
