1IOF

X-RAY CRYSTALLINE STRUCTURES OF PYRROLIDONE CARBOXYL PEPTIDASE FROM A HYPERTHERMOPHILE, PYROCOCCUS FURIOSUS, AND ITS CYS-FREE MUTANT

Summary for 1IOF

• Entry DOI: 10.2210/pdb1iof/pdb
• Related: 1IOI
• Descriptor: PYRROLIDONE CARBOXYL PEPTIDASE (2 entities in total)
• Functional Keywords: pgp-i, pyroglutamyl-peptidase i, pcp, protease, pyrococcus furiosus, archaea, hydrolase
• Biological source: Pyrococcus furiosus
• Total number of polymer chains: 4
• Total formula weight: 91407.13

Authors

Tanaka, H.,Chinami, M.,Ota, M.,Tsukihara, T.,Yutani, K. (deposition date: 2001-03-09, release date: 2001-03-21, Last modification date: 2023-10-25)

Primary citation

Tanaka, H.,Chinami, M.,Mizushima, T.,Ogasahara, K.,Ota, M.,Tsukihara, T.,Yutani, K.
X-ray crystalline structures of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus, and its cys-free mutant.
J.Biochem., 130:107-118, 2001

PubMed Abstract: 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.

PubMed: 11432786
DOI: 10.1093/oxfordjournals.jbchem.a002948

Experimental method

X-RAY DIFFRACTION (2.2 Å)