8RC6

Cryo-EM structure of hexameric BTB domain of Drosophila CG6765 protein

Summary for 8RC6

• Entry DOI: 10.2210/pdb8rc6/pdb
• EMDB information: 19049
• Descriptor: BTB domain of CG6765 protein (1 entity in total)
• Functional Keywords: dna-binding, transcription regulation, oligomerization, transcription
• Biological source: Drosophila melanogaster (fruit fly)
• Total number of polymer chains: 6
• Total formula weight: 87260.89

Authors

Bonchuk, A.N.,Naschberger, A.,Baradaran, R. (deposition date: 2023-12-06, release date: 2024-09-11)

Primary citation

Bonchuk, A.N.,Balagurov, K.I.,Baradaran, R.,Boyko, K.M.,Sluchanko, N.N.,Khrustaleva, A.M.,Burtseva, A.D.,Arkova, O.V.,Khalisova, K.K.,Popov, V.O.,Naschberger, A.,Georgiev, P.G.
The Arthropoda-specific Tramtrack group BTB protein domains use previously unknown interface to form hexamers.
Elife, 13:-, 2024

PubMed Abstract: BTB (Bric-a-brack, Tramtrack and Broad Complex) is a diverse group of protein-protein interaction domains found within metazoan proteins. Transcription factors contain a dimerizing BTB subtype with a characteristic N-terminal extension. The Tramtrack group (TTK) is a distinct type of BTB domain, which can multimerize. Single-particle cryo-EM microscopy revealed that the TTK-type BTB domains assemble into a hexameric structure consisting of three canonical BTB dimers connected through a previously uncharacterized interface. We demonstrated that the TTK-type BTB domains are found only in Arthropods and have undergone lineage-specific expansion in modern insects. The genome encodes 24 transcription factors with TTK-type BTB domains, whereas only four have non‑TTK‑type BTB domains. Yeast two-hybrid analysis revealed that the TTK-type BTB domains have an unusually broad potential for heteromeric associations presumably through dimer-dimer interaction interface. Thus, the TTK-type BTB domains are a structurally and functionally distinct group of protein domains specific to Arthropodan transcription factors.

PubMed: 39221775
DOI: 10.7554/eLife.96832

Experimental method

ELECTRON MICROSCOPY (3.3 Å)