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PDBsum entry 1nyc
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Hydrolase inhibitor
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PDB id
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1nyc
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PDB id:
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| Name: |
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Hydrolase inhibitor
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Title:
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Staphostatins resemble lipocalins, not cystatins in fold.
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Structure:
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Cysteine protease inhibitor. Chain: a, b. Synonym: staphostatin b. Engineered: yes
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Source:
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Staphylococcus aureus subsp. Aureus. Organism_taxid: 196620. Strain: mw2. Gene: staphostatin b (sspc). Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.40Å
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R-factor:
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0.202
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R-free:
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0.226
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Authors:
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M.Rzychon,R.Filipek,A.Sabat,K.Kosowska,A.Dubin,J.Potempa,M.Bochtler
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Key ref:
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M.Rzychon
et al.
(2003).
Staphostatins resemble lipocalins, not cystatins in fold.
Protein Sci,
12,
2252-2256.
PubMed id:
DOI:
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Date:
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12-Feb-03
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Release date:
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30-Sep-03
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PROCHECK
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Headers
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References
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Q7A189
(SSPC_STAAW) -
Staphostatin B from Staphylococcus aureus (strain MW2)
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Seq:
Struc:
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109 a.a.
111 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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DOI no:
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Protein Sci
12:2252-2256
(2003)
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PubMed id:
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Staphostatins resemble lipocalins, not cystatins in fold.
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M.Rzychon,
R.Filipek,
A.Sabat,
K.Kosowska,
A.Dubin,
J.Potempa,
M.Bochtler.
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ABSTRACT
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Staphostatins are the endogenous inhibitors of the major secreted cysteine
proteases of Staphylococcus aureus, the staphopains. Here, we present the 1.4 A
crystal structure of staphostatin B and show that the fold can be described as a
fully closed, highly sheared eight-stranded beta-barrel. Thus, staphostatin B is
related to beta-barrel domains that are involved in the inhibition or regulation
of proteases of various catalytic types and to the superfamily of
lipocalins/cytosolic fatty acid binding proteins. Unexpectedly for a cysteine
protease inhibitor, staphostatin B is not significantly similar to cystatins.
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Selected figure(s)
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Figure 3.
Figure 3. Stereo C  trace of
staphostatin B (continuous lines) and of fatty acid binding
protein from human muscle (1HMT [PDB]
), the closest lipocalin-like structural neighbor of
staphostatins (broken lines). The ligand in 1HMT [PDB]
, stearic acid, is shown in ball-and-stick representation.
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The above figure is
reprinted
by permission from the Protein Society:
Protein Sci
(2003,
12,
2252-2256)
copyright 2003.
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Figure was
selected
by an automated process.
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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.Kantyka,
K.Plaza,
J.Koziel,
D.Florczyk,
H.R.Stennicke,
I.B.Thogersen,
J.J.Enghild,
G.A.Silverman,
S.C.Pak,
and
J.Potempa
(2011).
Inhibition of Staphylococcus aureus cysteine proteases by human serpin potentially limits staphylococcal virulence.
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Biol Chem,
392,
483-489.
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R.F.Thornton,
T.F.Kagawa,
P.W.O'Toole,
and
J.C.Cooney
(2010).
The dissemination of C10 cysteine protease genes in Bacteroides fragilis by mobile genetic elements.
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BMC Microbiol,
10,
122.
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B.Władyka,
and
K.Pustelny
(2008).
Regulation of bacterial protease activity.
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Cell Mol Biol Lett,
13,
212-229.
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G.Dubin,
B.Wladyka,
J.Stec-Niemczyk,
D.Chmiel,
M.Zdzalik,
A.Dubin,
and
J.Potempa
(2007).
The staphostatin family of cysteine protease inhibitors in the genus Staphylococcus as an example of parallel evolution of protease and inhibitor specificity.
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Biol Chem,
388,
227-235.
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J.Otlewski,
F.Jelen,
M.Zakrzewska,
and
A.Oleksy
(2005).
The many faces of protease-protein inhibitor interaction.
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EMBO J,
24,
1303-1310.
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M.A.Meehl,
J.S.Pinkner,
P.J.Anderson,
S.J.Hultgren,
and
M.G.Caparon
(2005).
A novel endogenous inhibitor of the secreted streptococcal NAD-glycohydrolase.
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PLoS Pathog,
1,
e35.
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T.F.Kagawa,
P.W.O'toole,
and
J.C.Cooney
(2005).
SpeB-Spi: a novel protease-inhibitor pair from Streptococcus pyogenes.
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Mol Microbiol,
57,
650-666.
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G.Dubin,
J.Stec-Niemczyk,
T.Dylag,
J.Silberring,
A.Dubin,
and
J.Potempa
(2004).
Characterisation of a highly specific, endogenous inhibitor of cysteine protease from Staphylococcus epidermidis, a new member of the staphostatin family.
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Biol Chem,
385,
543-546.
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G.Dubin,
M.Krajewski,
G.Popowicz,
J.Stec-Niemczyk,
M.Bochtler,
J.Potempa,
A.Dubin,
and
T.A.Holak
(2003).
A novel class of cysteine protease inhibitors: solution structure of staphostatin A from Staphylococcus aureus.
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Biochemistry,
42,
13449-13456.
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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
