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| Appolaire, Alexandre; Rosenbaum, Eva; Dura, M. Asuncion; Colombo, Matteo; Marty, Vincent; Savoye, Marjolaine Noirclerc; Godfroy, Anne; Schoehn, Guy; Girard, Eric; Gabel, Frank; Franzetti, Bruno. |
| Tetrahedral (TET) aminopeptidases are large polypeptide destruction machines present in prokaryotes and eukaryotes. Here, the rules governing their assembly into hollow 12-subunit tetrahedrons are addressed by using TET2 from Pyrococcus horikoshii (PhTET2) as a model. Point mutations allowed the capture of a stable, catalytically active precursor. Small angle x- ray scattering revealed that it is a dimer whose architecture in solution is identical to that determined by x- ray crystallography within the fully assembled TET particle. Small angle x- ray scattering also showed that the reconstituted PhTET2 dodecameric particle displayed the same quaternary structure and thermal stability as the wild-type complex. The PhTET2 assembly intermediates were... |
| Tipo: Text |
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| Ano: 2013 |
URL: http://archimer.ifremer.fr/doc/00177/28820/27491.pdf |
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