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The structure of the Pfp1 protease from the hyperthermophilic archaeon Thermococcus thioreducens in two crystal forms

Published on Sep 1, 2017
· DOI :10.1107/S2059798317010622
Steven B. Larson13
Estimated H-index: 13
(UCI: University of California, Irvine),
Alexander McPherson53
Estimated H-index: 53
(UCI: University of California, Irvine)
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Abstract
The Pfp1 protease, a cysteine protease of unknown specificity from the hyperthermophilic archaeon Thermococcus thioreducens, was crystallized in two distinctive crystal forms: from concentrated citrate in one case and PEG in the other. X-ray data were collected from both crystal forms at room temperature to about 1.9 A resolution using a laboratory source and detector, and the structures were solved by molecular replacement using the Pfp1 protease from Pyrococcus horikoshii as the search model. In the T. thioreducens protease structures, Cys18 residues on adjacent molecules in the asymmetric units form intermolecular disulfide bonds, thereby yielding hexamers composed of three cross-linked, quasi-dyad-related dimers with crystallographically exact threefold axes and exhibiting almost exact 32 symmetry. The corresponding residue in P. horikoshii Pfp1 is Tyr18. An individual active site containing Cys100 and His101 also includes a Glu74 residue contributed by a quasi-twofold-related, non-cross-linked subunit. Two catalytic triads are therefore closely juxtaposed about the quasi-twofold axis at the interface of these subunits, and are relatively sequestered within the hexamer cavity. The cysteine in the active site is observed to be oxidized in both of the crystal forms that were studied.
  • References (13)
  • Citations (1)
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References13
Newest
Published on Mar 3, 2016in Prion1.60
Kiran Aslam2
Estimated H-index: 2
(Purdue University),
Tony R. Hazbun17
Estimated H-index: 17
(Purdue University)
ABSTRACTAmong different types of protein aggregation, amyloids are a biochemically well characterized state of protein aggregation that are associated with a large number of neurodegenerative diseases including Parkinson's disease, Alzheimer and Creutzfeldt-Jakob disease. Yeast, Saccharomyces cerevisiae is an insightful model to understand the underlying mechanism of protein aggregation. Many yeast molecular chaperones can modulate aggregation and misfolding of proteins including α-Syn and the S...
Published on Jan 1, 2016in Biochemical Journal4.33
Hyo Jung Kim9
Estimated H-index: 9
(SNU: Seoul National University),
Ae-Ran Kwon4
Estimated H-index: 4
(Daegu Haany University),
Bong-Jin Lee23
Estimated H-index: 23
(SNU: Seoul National University)
The DJ-1/ThiJ/ Pf pI superfamily is a group of proteins found in diverse organisms. This superfamily includes versatile proteins, such as proteases, chaperones, heat-shock proteins and human Parkinson's disease protein. Most members of the DJ-1/ThiJ/ Pf pI superfamily are oligomers and are classified into subfamilies depending on discriminating quaternary structures (DJ-1, YhbO and Hsp types). SAV1875, a conserved protein from Staphylococcus aureus , is a member of the YhbO-type subfamily. Howev...
Published on Aug 1, 2014in Eukaryotic Cell
Sylvia Siersleben1
Estimated H-index: 1
(Leibniz Association),
Daniel Penselin4
Estimated H-index: 4
(Leibniz Association)
+ 2 AuthorsWolfgang Knogge18
Estimated H-index: 18
(Leibniz Association)
Scald caused by Rhynchosporium commune is an important foliar disease of barley. Insertion mutagenesis of R. commune generated a nonpathogenic fungal mutant which carries the inserted plasmid in the upstream region of a gene named PFP1. The characteristic feature of the gene product is an Epc-N domain. This motif is also found in homologous proteins shown to be components of histone acetyltransferase (HAT) complexes of fungi and animals. Therefore, PFP1 is suggested to be the subunit of a HAT co...
Published on Dec 15, 2007in Journal of Bacteriology3.23
Jad Abdallah11
Estimated H-index: 11
(University of Paris),
Teresa Caldas11
Estimated H-index: 11
(University of Paris)
+ 2 AuthorsGilbert Richarme24
Estimated H-index: 24
(University of Paris)
YhbO is a member of the DJ-1/ThiJ/Pfp1 superfamily, which includes chaperones, peptidases, and the Parkinson's disease protein DJ-1. A yhbO-disrupted mutant of Escherichia coli is highly sensitive to oxidative, thermal, UV, and pH stresses, and the putative nucleophilic cysteine C104 of YhbO is required for stress resistance. These results suggest that YhbO affects a central process in stress management.
Elena V. Pikuta14
Estimated H-index: 14
,
Damien Marsic12
Estimated H-index: 12
(UAH: University of Alabama in Huntsville)
+ 6 AuthorsRichard B. Hoover18
Estimated H-index: 18
A hyperthermophilic, sulfur-reducing, organo-heterotrophic archaeon, strain OGL-20PT, was isolated from ‘black smoker’ chimney material from the Rainbow hydrothermal vent site on the Mid-Atlantic Ridge (36.2°N, 33.9°W). The cells of strain OGL-20PT have an irregular coccoid shape and are motile with a single flagellum. Growth was observed within a pH range of 5.0−8.5 (optimum pH 7.0), an NaCl concentration range of 1–5 % (w/v) (optimum 3 %) and a temperature range of 55–94 °C (optimum 83–85 °C)....
Published on Jul 1, 2006in Fems Microbiology Letters1.99
Sylvain Eschenlauer9
Estimated H-index: 9
(Glas.: University of Glasgow),
Graham H. Coombs61
Estimated H-index: 61
(Glas.: University of Glasgow),
Jeremy C. Mottram61
Estimated H-index: 61
(Glas.: University of Glasgow)
Pyrococcus furiosus protease I (PFPI) is a multimeric cysteine peptidase from P. furiosus. Genome analyses indicate that orthologues are present in rather few other organisms, including Dictyostelium discoideum and several bacteria, Archaea and plants. An open reading frame (ORF) coding for a PFPI-like protein (PFP1) was identified in Leishmania major and Leishmania mexicana and full-length spliced and polyadenylated PFP1 mRNA detected for both species. Vestiges of a PFPI-like gene could also be...
Published on Jan 1, 2002in Archaea3.09
Donald E. Ward5
Estimated H-index: 5
,
Keith R. Shockley14
Estimated H-index: 14
+ 4 AuthorsRobert M. Kelly51
Estimated H-index: 51
Proteases are found in every cell, where they recognize and break down unneeded or abnormal polypeptides or peptide-based nutrients within or outside the cell. Genome sequence data can be used to compare proteolytic enzyme inventories of different organisms as they relate to physiological needs for protein modification and hydrolysis. In this review, we exploit genome sequence data to compare hyperthermophilic microorganisms from the euryarchaeotal genus Pyrococcus, the crenarchaeote Sulfolobus ...
Published on Jan 1, 2001in Methods in Enzymology1.86
Lara S Chang3
Estimated H-index: 3
,
Paula M Hicks4
Estimated H-index: 4
,
Robert M. Kelly51
Estimated H-index: 51
Publisher Summary Pyrococcus furiosus is a hyperthermophilic archaeon from the order Thermococcales capable of growth on a variety of proteinaceous and carbohydrate-containing substrates. Analysis of gelatin-containing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDSPAGE) gels indicates that at least 11 endoproteinases are active in the cell extracts of this organism 2'3 and the following proteases have been characterized: protease I (PfpI), pyrolysin, proteasome, prolyl oligopepti...
Published on Aug 1, 1999
Alexander McPherson53
Estimated H-index: 53
The history and character of macromolecular crystals principles of macromolecular structure and the applications of x-ray crystallography the purification and characterization of biological macromolecules some physical and energetic principles practical procedures for macromolecular crystallization important considerations in macromolecular crystallization strategies and special approaches in growing crystals impurities, defects, and crystal quality the mechanisms and kinetics of macromolecular ...
Published on Jan 1, 1997in Applied and Environmental Microbiology4.08
Sheryl B. Halio3
Estimated H-index: 3
,
Michael W. Bauer10
Estimated H-index: 10
+ 2 AuthorsRobert M. Kelly51
Estimated H-index: 51
The hyperthermophilic archaeon Pyrococcus furiosus grows optimally at 100(deg)C by the fermentation of peptides and carbohydrates. From this organism, we have purified to homogeneity an intracellular protease, previously designated PfpI (P. furiosus protease I) (S. B. Halio, I. I. Blumentals, S. A. Short, B. M. Merrill, and R. M. Kelly, J. Bacteriol. 178:2605-2612, 1996). The protease contains a single subunit with a molecular mass of approximately 19 kDa and exists in at least two functional co...