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PDBsum entry 1ioi
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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X-Ray crystalline structures of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus, And its cys-Free mutant.
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Authors
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H.Tanaka,
M.Chinami,
T.Mizushima,
K.Ogasahara,
M.Ota,
T.Tsukihara,
K.Yutani.
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Ref.
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J Biochem (tokyo), 2001,
130,
107-118.
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PubMed id
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Abstract
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In order to elucidate the mechanism of the thermostability of proteins from
hyperthermophiles, X-ray crystalline structures of pyrrolidone carboxyl
peptidase from a hyperthermophile, Pyrococcus furiosus (PfPCP), and its mutant
protein with Ser substituted at Cys142 and Cys188 were determined at 2.2 and 2.7
A resolution, respectively. The obtained structures were compared with those
previously reported for pyrrolidone carboxyl peptidases from a
hyperthermophilie, Thermococcus litoralis (TlPCP), and from a mesophile,
Bacillus amyloliquefaciens (BaPCP). The PfPCP structure is a tetramer of four
identical subunits similar to that of the TlPCP and BaPCP. The largest
structural changes among the three PCPs were detected in the C-terminal
protrusion, which interacts with that of another subunit. A comparison of the
three structures indicated that the high stability of PfPCP is caused by
increases in hydrophobic interactions and hydrogen bonds, the formation of an
intersubunit ion-pair network, and improvement to an ideal conformation. On the
basis of the structures of the three proteins, it can be concluded that PfPCP
does not have any special factors responsible for its extremely high stability
and that the conformational structure of PfPCP is superior in its combination of
positive and negative stabilizing factors compared with BaPCP.
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