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PDBsum entry 2z9i
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284 a.a.
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269 a.a.
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260 a.a.
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Crystal structure of rv0983 from mycobacterium tuberculosis- proteolytically active form
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Structure:
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Probable serine protease pepd. Chain: a, b, c. Fragment: residues in database 149-464. Synonym: serine proteinase, mtb32b. Sveqv. Chain: d, e, f. Gatv. Chain: g, h, i
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Source:
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Mycobacterium tuberculosis. Organism_taxid: 1773. Other_details: autolytic products. Other_details: autolytic products
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Resolution:
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2.00Å
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R-factor:
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0.228
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R-free:
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0.273
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Authors:
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S.K.Palaninathan,N.N.Mohamedmohaideen,J.C.Sacchettini
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Key ref:
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N.N.Mohamedmohaideen
et al.
(2008).
Structure and function of the virulence-associated high-temperature requirement A of Mycobacterium tuberculosis.
Biochemistry,
47,
6092-6102.
PubMed id:
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Date:
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20-Sep-07
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Release date:
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10-Jun-08
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PROCHECK
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Headers
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References
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O53896
(O53896_MYCTU) -
Serine protease PepD from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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Seq:
Struc:
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464 a.a.
284 a.a.
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Biochemistry
47:6092-6102
(2008)
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PubMed id:
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Structure and function of the virulence-associated high-temperature requirement A of Mycobacterium tuberculosis.
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N.N.Mohamedmohaideen,
S.K.Palaninathan,
P.M.Morin,
B.J.Williams,
M.Braunstein,
S.E.Tichy,
J.Locker,
D.H.Russell,
W.R.Jacobs,
J.C.Sacchettini.
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ABSTRACT
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The high-temperature requirement A (HtrA) family of serine proteases has been
shown to play an important role in the environmental and cellular stress damage
control system in Escherichia coli. Mycobacterium tuberculosis ( Mtb) has three
putative HtrA-like proteases, HtrA1, HtrA2, and HtrA3. The deletion of htrA2
gives attenuated virulence in a mouse model of TB. Biochemical analysis reveals
that HtrA2 can function both as a protease and as a chaperone. The
three-dimensional structure of HtrA2 determined at 2.0 A resolution shows that
the protease domains form the central core of the trimer and the PDZ domains
extend to the periphery. Unlike E. coli DegS and DegP, the protease is naturally
active due to the formation of the serine protease-like catalytic triad and its
uniquely designed oxyanion hole. Both protease and PDZ binding pockets of each
HtrA2 molecule are occupied by autoproteolytic peptide products and reveal clues
for a novel autoregulatory mechanism that might have significant importance in
HtrA-associated virulence of Mtb.
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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.Clausen,
M.Kaiser,
R.Huber,
and
M.Ehrmann
(2011).
HTRA proteases: regulated proteolysis in protein quality control.
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Nat Rev Mol Cell Biol,
12,
152-162.
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C.L.Galindo,
J.Sha,
S.T.Moen,
S.L.Agar,
M.L.Kirtley,
S.M.Foltz,
L.J.McIver,
E.V.Kozlova,
H.R.Garner,
and
A.K.Chopra
(2010).
Comparative Global Gene Expression Profiles of Wild-Type Yersinia pestis CO92 and Its Braun Lipoprotein Mutant at Flea and Human Body Temperatures.
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Comp Funct Genomics,
(),
342168.
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M.J.White,
H.He,
R.M.Penoske,
S.S.Twining,
and
T.C.Zahrt
(2010).
PepD participates in the mycobacterial stress response mediated through MprAB and SigE.
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J Bacteriol,
192,
1498-1510.
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T.Krojer,
J.Sawa,
R.Huber,
and
T.Clausen
(2010).
HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues.
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Nat Struct Mol Biol,
17,
844-852.
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PDB codes:
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V.Sintchenko,
S.Anthony,
X.H.Phan,
F.Lin,
and
E.W.Coiera
(2010).
A PubMed-wide associational study of infectious diseases.
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PLoS One,
5,
e9535.
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B.O.Cezairliyan,
and
R.T.Sauer
(2009).
Control of Pseudomonas aeruginosa AlgW protease cleavage of MucA by peptide signals and MucB.
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Mol Microbiol,
72,
368-379.
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J.Sohn,
R.A.Grant,
and
R.T.Sauer
(2009).
OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism.
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Structure,
17,
1411-1421.
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PDB codes:
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J.Sohn,
and
R.T.Sauer
(2009).
OMP peptides modulate the activity of DegS protease by differential binding to active and inactive conformations.
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Mol Cell,
33,
64-74.
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T.R.Ioerger,
and
J.C.Sacchettini
(2009).
Structural genomics approach to drug discovery for Mycobacterium tuberculosis.
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Curr Opin Microbiol,
12,
318-325.
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O.H.Vandal,
L.M.Pierini,
D.Schnappinger,
C.F.Nathan,
and
S.Ehrt
(2008).
A membrane protein preserves intrabacterial pH in intraphagosomal Mycobacterium tuberculosis.
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Nat Med,
14,
849-854.
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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
