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PDBsum entry 2z9i
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Contents |
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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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References listed in PDB file
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Key reference
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Title
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Structure and function of the virulence-Associated high-Temperature requirement a of mycobacterium tuberculosis.
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Authors
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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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Ref.
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Biochemistry, 2008,
47,
6092-6102.
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PubMed id
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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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