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-Structure paper
タイトル | An archaeal peptidase assembles into two different quaternary structures: A tetrahedron and a giant octahedron. |
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ジャーナル・号・ページ | J Biol Chem, Vol. 281, Issue 47, Page 36327-36337, Year 2006 |
掲載日 | 2006年11月24日 |
![]() | Guy Schoehn / Frédéric M D Vellieux / M Asunción Durá / Véronique Receveur-Bréchot / Céline M S Fabry / Rob W H Ruigrok / Christine Ebel / Alain Roussel / Bruno Franzetti / ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (単粒子) / X線回折 |
解像度 | 3.08 - 15.0 Å |
構造データ | ![]() EMDB-1188: ![]() EMDB-1189: ![]() PDB-2cf4: |
化合物 | ![]() ChemComp-CO: |
由来 |
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![]() | HYDROLASE / AMINOPEPTIDASE / METALLOPROTEIN / HYPERTHERMOPHILE / ARCHAEA / TETRAHEDRAL |