Small-angle neutron scattering reveals the assembly mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase.

Abstract : The specific self-association of proteins into oligomeric complexes is a common phenomenon in biological systems to optimize and regulate their function. However, de novo structure determination of these important complexes is often very challenging for atomic-resolution techniques. Furthermore, in the case of homo-oligomeric complexes, or complexes with very similar building blocks, the respective positions of subunits and their assembly pathways are difficult to determine using many structural biology techniques. Here, an elegant and powerful approach based on small-angle neutron scattering is applied, in combination with deuterium labelling and contrast variation, to elucidate the oligomeric organization of the quaternary structure and the assembly pathways of 468 kDa, hetero-oligomeric and symmetric Pyrococcus horikoshii TET2-TET3 aminopeptidase complexes. The results reveal that the topology of the PhTET2 and PhTET3 dimeric building blocks within the complexes is not casual but rather suggests that their quaternary arrangement optimizes the catalytic efficiency towards peptide substrates. This approach bears important potential for the determination of quaternary structures and assembly pathways of large oligomeric and symmetric complexes in biological systems.
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Acta Crystallographica Section D: Biological Crystallography, International Union of Crystallography, 2014, 70 (Pt 11), pp.2983-93
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http://hal.univ-grenoble-alpes.fr/hal-01131157
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Soumis le : vendredi 13 mars 2015 - 09:26:57
Dernière modification le : lundi 2 avril 2018 - 18:30:01

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Alexandre Appolaire, Eric Girard, Matteo Colombo, M Asunción Durá, Martine Moulin, et al.. Small-angle neutron scattering reveals the assembly mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase.. Acta Crystallographica Section D: Biological Crystallography, International Union of Crystallography, 2014, 70 (Pt 11), pp.2983-93. 〈hal-01131157〉

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