期刊
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
卷 70, 期 -, 页码 2983-2993出版社
WILEY-BLACKWELL
DOI: 10.1107/S1399004714018446
关键词
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资金
- Agence Nationale de la Recherche [BLAN-07-3204002, ANR-12-BSV8-0019-01, ANR-11-JSV5-003-01]
- French Ministry for Research and Technology
- French National Research Agency
- EPSRC [EP/C015452/1]
- EU [RII3-CT-2003-505925]
- Agence Nationale de la Recherche (ANR) [ANR-12-BSV8-0019] Funding Source: Agence Nationale de la Recherche (ANR)
- Engineering and Physical Sciences Research Council [EP/C015452/1] Funding Source: researchfish
- EPSRC [EP/C015452/1] Funding Source: UKRI
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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