7MWH

Crystal structure of BAZ2A with DNA

Summary for 7MWH

• Entry DOI: 10.2210/pdb7mwh/pdb
• Descriptor: Bromodomain adjacent to zinc finger domain protein 2A, DNA (5'-D(*CP*GP*GP*AP*AP*TP*GP*TP*AP*GP*GP*C)-3'), DNA (5'-D(*GP*CP*CP*TP*AP*(5CM)P*AP*TP*TP*CP*CP*G)-3'), ... (5 entities in total)
• Functional Keywords: mbd, tam, structural genomics, structural genomics consortium, sgc, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 35291.69

Authors

Liu, K.,Dong, A.,Li, Y.,Loppnau, P.,Edwards, A.M.,Arrowsmith, C.H.,Min, J.,Structural Genomics Consortium (SGC) (deposition date: 2021-05-17, release date: 2022-08-31, Last modification date: 2023-10-25)

Primary citation

Feng, Y.,Chen, S.,Zhou, M.,Zhang, J.,Min, J.,Liu, K.
Crystal structure of the BAZ2B TAM domain.
Heliyon, 8:e09873-e09873, 2022

PubMed Abstract: BAZ2B is a regulatory subunit of the ISWI (Imitation Switch) remodeling complex and engages in nucleosome remodeling. Loss-of-function and haploinsufficiency of BAZ2B are associated with different diseases. BAZ2B is a large multidomain protein. In addition to the epigenetic reader domains plant homeodomain (PHD) and bromodomain (BRD), BAZ2B also has a Tip5/ARBP/MBD (TAM) domain. Sequence alignment revealed that the TAM domains of BAZ2A and BAZ2B share 53% sequence identity. How the BAZ2A TAM domain bound with DNA has been characterized recently, however, the DNA binding ability and methylation preference, as well as the structural basis of the BAZ2B TAM domain are not studied yet. In this study, we measured the DNA binding affinity of the TAM domain of BAZ2B, and also determined its apo crystal structure. We found that the TAM domains of BAZ2A and BAZ2B adopt almost the same fold, and like BAZ2A, the BAZ2B TAM domain also binds to dsDNA without methyl-cytosine preference, implying that the BAZ2B TAM domain might recognize DNA in a similar binding mode to that of the BAZ2A TAM domain. These results provide clues for the biological function study of BAZ2B in the future.

PubMed: 35865993
DOI: 10.1016/j.heliyon.2022.e09873

Experimental method

X-RAY DIFFRACTION (2.28 Å)