An archaeal peptidase assembles into two different quaternary structures: A tetrahedron and a giant octahedron
Cellular proteolysis involves large oligomeric peptidases that play key roles in the regulation of many cellular processes. The cobalt-activated peptidase TET1 from the hyperthermophilic Archaea Pyrococcus horikoshii (PhTET1) was found to assemble as a 12-subunit tetrahedron and as a 24-subunit octa...
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| Veröffentlicht in: | The Journal of biological chemistry 2006-11, Vol.281 (47), p.36327-36337 |
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| container_title | The Journal of biological chemistry |
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| creator | Schoehn, Guy Vellieux, Frédéric M D Asunción Durá, M Receveur-Bréchot, Véronique Fabry, Céline M S Ruigrok, Rob W H Ebel, Christine Roussel, Alain Franzetti, Bruno |
| description | Cellular proteolysis involves large oligomeric peptidases that play key roles in the regulation of many cellular processes. The cobalt-activated peptidase TET1 from the hyperthermophilic Archaea Pyrococcus horikoshii (PhTET1) was found to assemble as a 12-subunit tetrahedron and as a 24-subunit octahedral particle. Both quaternary structures were solved by combining x-ray crystallography and cryoelectron microscopy data. The internal organization of the PhTET1 particles reveals highly self-compartmentalized systems made of networks of access channels extended by vast catalytic chambers. The two edifices display aminopeptidase activity, and their organizations indicate substrate navigation mechanisms different from those described in other large peptidase complexes. Compared with the tetrahedron, the octahedron forms a more expanded hollow structure, representing a new type of giant peptidase complex. PhTET1 assembles into two different quaternary structures because of quasi-equivalent contacts that previously have only been identified in viral capsids. |
| doi_str_mv | 10.1074/jbc.M604417200 |
| format | Article |
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The cobalt-activated peptidase TET1 from the hyperthermophilic Archaea Pyrococcus horikoshii (PhTET1) was found to assemble as a 12-subunit tetrahedron and as a 24-subunit octahedral particle. Both quaternary structures were solved by combining x-ray crystallography and cryoelectron microscopy data. The internal organization of the PhTET1 particles reveals highly self-compartmentalized systems made of networks of access channels extended by vast catalytic chambers. The two edifices display aminopeptidase activity, and their organizations indicate substrate navigation mechanisms different from those described in other large peptidase complexes. Compared with the tetrahedron, the octahedron forms a more expanded hollow structure, representing a new type of giant peptidase complex. PhTET1 assembles into two different quaternary structures because of quasi-equivalent contacts that previously have only been identified in viral capsids.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M604417200</identifier><identifier>PMID: 16973604</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Aminopeptidases ; Aminopeptidases - chemistry ; Aminopeptidases - metabolism ; Archaea ; Biochemistry, Molecular Biology ; Capsid ; Capsid - chemistry ; Catalysis ; Cryoelectron Microscopy ; Crystallography, X-Ray ; Dimerization ; Hydrolysis ; Life Sciences ; Models, Molecular ; Molecular Sequence Data ; Peptides ; Peptides - chemistry ; Protein Conformation ; Protein Structure, Quaternary ; Pyrococcus ; Pyrococcus - enzymology ; Pyrococcus horikoshii ; Sequence Homology, Amino Acid</subject><ispartof>The Journal of biological chemistry, 2006-11, Vol.281 (47), p.36327-36337</ispartof><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c319t-5a1733bf030c67e63d0784fc0a87615817f638d46bbd23b328d99a01ad1a6bd03</citedby><orcidid>0000-0002-1459-3201 ; 0000-0002-6912-500X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,777,781,882,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16973604$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00475651$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Schoehn, Guy</creatorcontrib><creatorcontrib>Vellieux, Frédéric M D</creatorcontrib><creatorcontrib>Asunción Durá, M</creatorcontrib><creatorcontrib>Receveur-Bréchot, Véronique</creatorcontrib><creatorcontrib>Fabry, Céline M S</creatorcontrib><creatorcontrib>Ruigrok, Rob W H</creatorcontrib><creatorcontrib>Ebel, Christine</creatorcontrib><creatorcontrib>Roussel, Alain</creatorcontrib><creatorcontrib>Franzetti, Bruno</creatorcontrib><title>An archaeal peptidase assembles into two different quaternary structures: A tetrahedron and a giant octahedron</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Cellular proteolysis involves large oligomeric peptidases that play key roles in the regulation of many cellular processes. The cobalt-activated peptidase TET1 from the hyperthermophilic Archaea Pyrococcus horikoshii (PhTET1) was found to assemble as a 12-subunit tetrahedron and as a 24-subunit octahedral particle. Both quaternary structures were solved by combining x-ray crystallography and cryoelectron microscopy data. The internal organization of the PhTET1 particles reveals highly self-compartmentalized systems made of networks of access channels extended by vast catalytic chambers. The two edifices display aminopeptidase activity, and their organizations indicate substrate navigation mechanisms different from those described in other large peptidase complexes. Compared with the tetrahedron, the octahedron forms a more expanded hollow structure, representing a new type of giant peptidase complex. PhTET1 assembles into two different quaternary structures because of quasi-equivalent contacts that previously have only been identified in viral capsids.</description><subject>Amino Acid Sequence</subject><subject>Aminopeptidases</subject><subject>Aminopeptidases - chemistry</subject><subject>Aminopeptidases - metabolism</subject><subject>Archaea</subject><subject>Biochemistry, Molecular Biology</subject><subject>Capsid</subject><subject>Capsid - chemistry</subject><subject>Catalysis</subject><subject>Cryoelectron Microscopy</subject><subject>Crystallography, X-Ray</subject><subject>Dimerization</subject><subject>Hydrolysis</subject><subject>Life Sciences</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Peptides</subject><subject>Peptides - chemistry</subject><subject>Protein Conformation</subject><subject>Protein Structure, Quaternary</subject><subject>Pyrococcus</subject><subject>Pyrococcus - enzymology</subject><subject>Pyrococcus horikoshii</subject><subject>Sequence Homology, Amino Acid</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEFP3DAQhS1UxC6Ua4-VT5V6CMzEju30tkItIC3iAlJv0SSesFllk8V2QPx7UrHttXMZ6el7T09PiC8IFwhWX27r5uLOgNZoc4AjsURwKlMF_v4klgA5ZmVeuIU4jXEL8-kST8QCTWnV7FqKYTVICs2GmHq5533qPEWWFCPv6p6j7IY0yvQ6St-1LQceknyeKHEYKLzJmMLUpClw_CFXMnEKtGEfxjl08JLkU0ezYWzSQf4sjlvqI58f_pl4_PXz4eomW99f316t1lmjsExZQWiVqltQ0BjLRnmwTrcNkLMGC4e2Ncp5bera56pWufNlSYDkkUztQZ2J7x-5G-qrfeh2c9lqpK66Wa2rP9q8hC1MgS84s98-2H0YnyeOqdp1seG-p4HHKVbGoclRw39BLJ1WgHoGvx7Aqd6x_1fg7-zqHeKEhJI</recordid><startdate>20061124</startdate><enddate>20061124</enddate><creator>Schoehn, Guy</creator><creator>Vellieux, Frédéric M D</creator><creator>Asunción Durá, M</creator><creator>Receveur-Bréchot, Véronique</creator><creator>Fabry, Céline M S</creator><creator>Ruigrok, Rob W H</creator><creator>Ebel, Christine</creator><creator>Roussel, Alain</creator><creator>Franzetti, Bruno</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>7U9</scope><scope>C1K</scope><scope>H94</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0002-1459-3201</orcidid><orcidid>https://orcid.org/0000-0002-6912-500X</orcidid></search><sort><creationdate>20061124</creationdate><title>An archaeal peptidase assembles into two different quaternary structures: A tetrahedron and a giant octahedron</title><author>Schoehn, Guy ; 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| subjects | Amino Acid Sequence Aminopeptidases Aminopeptidases - chemistry Aminopeptidases - metabolism Archaea Biochemistry, Molecular Biology Capsid Capsid - chemistry Catalysis Cryoelectron Microscopy Crystallography, X-Ray Dimerization Hydrolysis Life Sciences Models, Molecular Molecular Sequence Data Peptides Peptides - chemistry Protein Conformation Protein Structure, Quaternary Pyrococcus Pyrococcus - enzymology Pyrococcus horikoshii Sequence Homology, Amino Acid |
| title | An archaeal peptidase assembles into two different quaternary structures: A tetrahedron and a giant octahedron |
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