2CF4
Pyrococcus horikoshii TET1 peptidase can assemble into a tetrahedron or a large octahedral shell
Summary for 2CF4
| Entry DOI | 10.2210/pdb2cf4/pdb |
| Descriptor | PROTEIN PH0519, COBALT (II) ION (2 entities in total) |
| Functional Keywords | aminopeptidase, metalloprotein, hyperthermophile, archaea, tetrahedral, hydrolase |
| Biological source | PYROCOCCUS HORIKOSHII |
| Total number of polymer chains | 1 |
| Total formula weight | 37324.95 |
| Authors | Vellieux, F.M.D.,Schoehn, G.,Dura, M.A.,Roussel, A.,Franzetti, B. (deposition date: 2006-02-15, release date: 2006-09-14, Last modification date: 2024-11-06) |
| Primary citation | Schoehn, G.,Vellieux, F.M.D.,Dura, M.A.,Receveur-Brechot, V.,Fabry, C.M.S.,Ruigrok, R.W.H.,Ebel, C.,Roussel, A.,Franzetti, B. An Archaeal Peptidase Assembles Into Two Different Quaternary Structures: A Tetrahedron and a Giant Octahedron. J.Biol.Chem., 281:36327-, 2006 Cited by PubMed Abstract: 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. PubMed: 16973604DOI: 10.1074/JBC.M604417200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.08 Å) |
Structure validation
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