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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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References listed in PDB file
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Key reference
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Title
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Staphostatins resemble lipocalins, Not cystatins in fold.
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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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Ref.
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Protein Sci, 2003,
12,
2252-2256.
[DOI no: ]
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PubMed id
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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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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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Secondary reference #1
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Title
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Identification of a novel maturation mechanism and restricted substrate specificity for the sspb cysteine protease of staphylococcus aureus.
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Authors
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I.Massimi,
E.Park,
K.Rice,
W.Muller-Esterl,
D.Sauder,
M.J.Mcgavin.
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Ref.
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J Biol Chem, 2002,
277,
41770-41777.
[DOI no: ]
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PubMed id
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Figure 5.
Fig. 5. Assay of SspA (  circle )
and SspB (  ) with
resorufin-labeled casein as substrate.
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Figure 10.
Fig. 10. Primary human keratinocytes after incubation for
7 h with medium alone (A) and medium supplemented with 10
µg/ml SspB (B) or 10 µg/ml SspB and 28 µM E-64
cysteine protease inhibitor (C).
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The above figures are
reproduced from the cited reference
with permission from the ASBMB
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Secondary reference #2
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Title
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Staphostatins: an expanding new group of proteinase inhibitors with a unique specificity for the regulation of staphopains, Staphylococcus spp. Cysteine proteinases.
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Authors
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M.Rzychon,
A.Sabat,
K.Kosowska,
J.Potempa,
A.Dubin.
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Ref.
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Mol Microbiol, 2003,
49,
1051-1066.
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PubMed id
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