3M52

Crystal structure of the BTB domain from the Miz-1/ZBTB17 transcription regulator

Summary for 3M52

• Entry DOI: 10.2210/pdb3m52/pdb
• Related: 3M4T 3M5B
• Descriptor: Zinc finger and BTB domain-containing protein 17, ZINC ION, ACETATE ION, ... (4 entities in total)
• Functional Keywords: btb domain, poz domain, btb/poz domain, miz-1, zinc finger protein 151, myc-interacting zinc finger protein, miz-1 protein, zfp151, zfp-151, znf151, miz1, zinc finger and btb domain-containing protein 17, zinc finger protein 60, protein-protein interaction domain, transcription regulator, transcription activator, zinc-finger protein, alpha/beta protein, developmental protein, dna-binding, metal-binding, nucleus, transcription, transcription regulation, zinc-finger, dna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q13105
• Total number of polymer chains: 2
• Total formula weight: 26380.29

Authors

Stogios, P.J.,Cuesta-Seijo, J.A.,Chen, L.,Prive, G.G. (deposition date: 2010-03-12, release date: 2010-06-09, Last modification date: 2023-09-06)

Primary citation

Stogios, P.J.,Cuesta-Seijo, J.A.,Chen, L.,Pomroy, N.C.,Prive, G.G.
Insights into Strand Exchange in BTB Domain Dimers from the Crystal Structures of FAZF and Miz1.
J.Mol.Biol., 400:983-997, 2010

PubMed Abstract: The BTB domain is a widely distributed protein-protein interaction motif that is often found at the N-terminus of zinc finger transcription factors. Previous crystal structures of BTB domains have revealed tightly interwound homodimers, with the N-terminus from one chain forming a two-stranded anti-parallel beta-sheet with a strand from the other chain. We have solved the crystal structures of the BTB domains from Fanconi anemia zinc finger (FAZF) and Miz1 (Myc-interacting zinc finger 1) to resolutions of 2.0 A and 2.6 A, respectively. Unlike previous examples of BTB domain structures, the FAZF BTB domain is a nonswapped dimer, with each N-terminal beta-strand associated with its own chain. As a result, the dimerization interface in the FAZF BTB domain is about half as large as in the domain-swapped dimers. The Miz1 BTB domain resembles a typical swapped BTB dimer, although it has a shorter N-terminus that is not able to form the interchain sheet. Using cysteine cross-linking, we confirmed that the promyelocytic leukemia zinc finger (PLZF) BTB dimer is strand exchanged in solution, while the FAZF BTB dimer is not. A phylogenic tree of the BTB fold based on both sequence and structural features shows that the common ancestor of the BTB domain in BTB-ZF (bric à brac, tramtrack, broad-complex zinc finger) proteins was a domain-swapped dimer. The differences in the N-termini seen in the FAZF and Miz1 BTB domains appear to be more recent developments in the structural evolution of the domain.

PubMed: 20493880
DOI: 10.1016/j.jmb.2010.05.028

Experimental method

X-RAY DIFFRACTION (2.59 Å)