 |
PDBsum entry 1srp
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Hydrolase (metalloprotease)
|
PDB id
|
|
|
|
1srp
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
|
|
|
|
|
Enzyme class:
|
|
E.C.3.4.24.40
- serralysin.
|
|
|
|
|
|
|
Reaction:
|
|
Preferential cleavage of bonds with hydrophobic residues in P1'.
|
|
|
|
|
|
Cofactor:
|
|
Zn(2+)
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
J Biochem (tokyo)
119:844-851
(1996)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Crystal structure of Serratia protease, a zinc-dependent proteinase from Serratia sp. E-15, containing a beta-sheet coil motif at 2.0 A resolution.
|
|
K.Hamada,
Y.Hata,
Y.Katsuya,
H.Hiramatsu,
T.Fujiwara,
Y.Katsube.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
The crystal structure of Serratia protease from Serratia sp. E-15 was solved by
the single isomorphous replacement method supplemented with anomalous scattering
effects from both the Zn atom in the native crystal and the Sm atom in the
derivative crystal, and refined at 2.0 A resolution to a crystallographic
R-factor of 0.194. The enzyme consists of N-terminal catalytic and C-terminal
beta-sandwich domains, as observed in alkaline protease from Pseudomonas
aeruginosa IFO3080. The catalytic domain with a five-stranded antiparallel
beta-sheet and five alpha-helices shares a basically common folding topology
with those of other zinc metalloendoproteases. The catalytic zinc ion at the
bottom of the active site cleft is ligated by His176, His180, His186, Tyr216,
and a water molecule in a distorted trigonalbipyramidal manner. The C-terminal
domain is a beta-strand-rich domain containing eighteen beta-strands and a short
alpha-helix, and has seven Ca2+ ions bound to calcium binding loops. An unusual
beta-sheet coil motif is observed in this domain, where the beta-strands and
calcium binding loops are alternately incorporated into an elliptical
right-handed spiral so as to form a two-layer untwisted beta-sandwich structure.
The Ca2+ ions in the C-terminal domain seem to be very important for the folding
and stability of the beta-sheet coil structure.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
N.M.Nirale,
and
M.D.Menon
(2010).
Topical formulations of serratiopeptidase: development and pharmacodynamic evaluation.
|
| |
Indian J Pharm Sci,
72,
65-71.
|
|
|
|
|
|
|
N.Aghajari,
F.Van Petegem,
V.Villeret,
J.P.Chessa,
C.Gerday,
R.Haser,
and
J.Van Beeumen
(2003).
Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases.
|
| |
Proteins,
50,
636-647.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
H.J.Kwon,
M.Haruki,
M.Morikawa,
K.Omori,
and
S.Kanaya
(2002).
Role of repetitive nine-residue sequence motifs in secretion, enzymatic activity, and protein conformation of a family I.3 lipase.
|
| |
J Biosci Bioeng,
93,
157-164.
|
|
|
|
|
|
|
N.Rashid,
Y.Shimada,
S.Ezaki,
H.Atomi,
and
T.Imanaka
(2001).
Low-temperature lipase from psychrotrophic Pseudomonas sp. strain KB700A.
|
| |
Appl Environ Microbiol,
67,
4064-4069.
|
|
|
|
|
|
|
J.Heringa,
and
W.R.Taylor
(1997).
Three-dimensional domain duplication, swapping and stealing.
|
| |
Curr Opin Struct Biol,
7,
416-421.
|
|
|
|
|
|
|
B.Kobe
(1996).
Leucines on a roll.
|
| |
Nat Struct Biol,
3,
977-980.
|
|
|
|
|
|
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
codes are
shown on the right.
|
|
Links
