PDBsum entry 1iof

Hydrolase

PDB id: 1iof

Contents

Protein chains

208 a.a. *

Waters ×168

* Residue conservation analysis

PDB id:

1iof

Name:

Hydrolase

Title:

X-ray crystalline structures of pyrrolidone carboxyl peptidase from a hyperthermophile, pyrococcus furiosus, and its cys-free mutant

Structure:

Pyrrolidone carboxyl peptidase. Chain: a, b, c, d. Engineered: yes

Source:

Pyrococcus furiosus. Organism_taxid: 2261. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Tetramer (from PQS)

Resolution:

2.20Å R-factor: 0.195 R-free: 0.232

Authors:

H.Tanaka,M.Chinami,M.Ota,T.Tsukihara,K.Yutani

Key ref:

H.Tanaka et al. (2001). X-ray crystalline structures of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus, and its cys-free mutant. J Biochem (tokyo), 130, 107-118. PubMed id: 11432786

Date:

09-Mar-01 Release date: 21-Mar-01

Protein chains

O73944  (PCP_PYRFU) -  Pyrrolidone-carboxylate peptidase from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

Seq: 208 a.a.

Struc: 208 a.a.

Enzyme reactions

• Enzyme class: E.C.3.4.19.3 - pyroglutamyl-peptidase I.
• Reaction: 5-oxoprolyl-peptide + H₂O = 5-oxoproline + peptide

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

J Biochem (tokyo) 130:107-118 (2001)

PubMed id: 11432786

X-ray crystalline structures of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus, and its cys-free mutant.

H.Tanaka, M.Chinami, T.Mizushima, K.Ogasahara, M.Ota, T.Tsukihara, K.Yutani.

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.