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Hydrolase (metalloproteinase)
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PDB id
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1akl
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Contents |
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* Residue conservation analysis
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Enzyme class:
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E.C.3.4.24.40
- Serralysin.
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Reaction:
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Preferential cleavage of bonds with hydrophobic residues in P1'.
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Cofactor:
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Zinc
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Gene Ontology (GO) functional annotation
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Cellular component
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extracellular region
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2 terms
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Biological process
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proteolysis
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1 term
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Biochemical function
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hydrolase activity
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7 terms
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J Biochem (tokyo)
118:474-479
(1995)
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PubMed id:
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Crystal structure of the unliganded alkaline protease from Pseudomonas aeruginosa IFO3080 and its conformational changes on ligand binding.
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H.Miyatake,
Y.Hata,
T.Fujii,
K.Hamada,
K.Morihara,
Y.Katsube.
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ABSTRACT
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The crystal structure of the unliganded alkaline protease from Pseudomonas
aeruginosa IFO3080 has been determined at 2.0 A resolution by the X-ray method.
The enzyme consists of N-terminal catalytic and C-terminal beta-helix domains.
On structural comparison between the present unliganded enzyme and structurally-
known liganded enzyme, some structural changes were observed around the active
site. In the unliganded enzyme, Y216 serves as the fifth ligand for the active
site zinc ion. On ligand binding, Y216 may move to form a hydrogen-bond with the
carbonyl oxygen of the P1 residue of a ligand peptide. D191 in the flexible
loop, Y190 to D196, over the active site cleft forms hydrogen-bonds with the
backbone atoms of the P1 and P2 residues of the ligand to close the entrance to
the cleft. The water molecule which is the fourth ligand for the zinc ion is
replaced by the carbonyl oxygen of the P1 residue. These structural changes
around the active site may reflect the substrate-binding mode during the
enzymatic reaction.
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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.Walasek,
and
J.F.Honek
(2005).
Nonnatural amino acid incorporation into the methionine 214 position of the metzincin Pseudomonas aeruginosa alkaline protease.
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BMC Biochem, 6,
21.
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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.
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Proteins, 50,
636-647.
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PDB codes:
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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.
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J Biosci Bioeng, 93,
157-164.
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J.D.Cronk,
J.A.Endrizzi,
M.R.Cronk,
J.W.O'neill,
and
K.Y.Zhang
(2001).
Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity.
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Protein Sci, 10,
911-922.
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PDB codes:
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D.Louis,
P.Sorlier,
and
J.Wallach
(1998).
Quantitation and enzymatic activity of the alkaline protease from Pseudomonas aeruginosa in culture supernatants from clinical strains.
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Clin Chem Lab Med, 36,
295-298.
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F.Grams,
V.Dive,
A.Yiotakis,
I.Yiallouros,
S.Vassiliou,
R.Zwilling,
W.Bode,
and
W.Stöcker
(1996).
Structure of astacin with a transition-state analogue inhibitor.
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Nat Struct Biol, 3,
671-675.
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PDB codes:
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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
codes are
shown on the right.
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Links
