2AQE
Structural and functional analysis of ada2 alpha swirm domain
Summary for 2AQE
Entry DOI | 10.2210/pdb2aqe/pdb |
Related | 2AQF |
NMR Information | BMRB: 6781 |
Descriptor | Transcriptional adaptor 2, Ada2 alpha (1 entity in total) |
Functional Keywords | helix-turn-helix, transcription |
Biological source | Mus musculus (house mouse) |
Total number of polymer chains | 1 |
Total formula weight | 10042.67 |
Authors | Qian, C.,Zhang, Q.,Zeng, L.,Zhou, M.-M. (deposition date: 2005-08-17, release date: 2005-12-13, Last modification date: 2024-05-22) |
Primary citation | Qian, C.,Zhang, Q.,Li, S.D.,Zeng, L.,Walsh, M.J.,Zhou, M.-M. Structure and chromosomal DNA binding of the SWIRM domain Nat.Struct.Mol.Biol., 12:1078-1085, 2005 Cited by PubMed Abstract: The evolutionarily conserved Swi3p, Rsc8p and Moira (SWIRM) domain is found in many chromosomal proteins involved in chromatin modifications or remodeling. Here we report the three-dimensional solution structure of the SWIRM domain from the human transcriptional adaptor ADA2alpha. The structure reveals a five-helix bundle consisting of two helix-turn-helix motifs connected by a central long helix, reminiscent of the histone fold. Using structural and biochemical analyses, we showed that the SWIRM domains of human ADA2alpha and SMARC2 bind to double-stranded and nucleosomal DNA, and we identified amino acid residues required for this function. We demonstrated that the ADA2alpha SWIRM domain is colocalized with lysine-acetylated histone H3 in the cell nucleus and that it potentiates the ACF remodeling activity by enhancing accessibility of nucleosomal linker DNA bound to histone H1. These data suggest a functional role of the SWIRM domain in chromatin remodeling. PubMed: 16299514DOI: 10.1038/nsmb1022 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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