2AQL

Crystal Structure of the MRG15 MRG domain

Summary for 2AQL

• Entry DOI: 10.2210/pdb2aql/pdb
• Descriptor: Mortality factor 4-like protein 1 (2 entities in total)
• Functional Keywords: helix hairpins, mrg domain, core binding domain, recombinase, dna binding, chromatin remodeling, dna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q9UBU8
• Total number of polymer chains: 2
• Total formula weight: 40144.16

Authors

Quiocho, F.A.,Bowman, B.R. (deposition date: 2005-08-18, release date: 2006-02-28, Last modification date: 2024-02-14)

Primary citation

Bowman, B.R.,Moure, C.M.,Kirtane, B.M.,Welschhans, R.L.,Tominaga, K.,Pereira-Smith, O.M.,Quiocho, F.A.
Multipurpose MRG domain involved in cell senescence and proliferation exhibits structural homology to a DNA-interacting domain.
Structure, 14:151-158, 2006

PubMed Abstract: The ubiquitous MRG/MORF family of proteins is involved in cell senescence, or the terminal loss of proliferative potential, a model for aging and tumor suppression at the cellular level. These proteins are defined by the approximately 20 kDa MRG domain that binds a plethora of transcriptional regulators and chromatin-remodeling factors, including the histone deacetylase transcriptional corepressor mSin3A and the novel nuclear protein PAM14, and they are also known components of the Tip60/NuA4 complex via interactions with the MRG binding protein (MRGBP). We present here the crystal structure of a prototypic MRG domain from human MRG15 whose core consists of two orthogonal helix hairpins. Despite the lack of sequence similarity, the core structure has surprisingly striking homology to a DNA-interacting domain of the tyrosine site-specific recombinases XerD, lambda integrase, and Cre. Site-directed mutagenesis studies based on the X-ray structure and bioinformatics identified key residues involved in the binding of PAM14 and MRGBP.

PubMed: 16407074
DOI: 10.1016/j.str.2005.08.019

Experimental method

X-RAY DIFFRACTION (2.3 Å)