4Q2J

A novel structure-based mechanism for DNA-binding of SATB1

Summary for 4Q2J

• Entry DOI: 10.2210/pdb4q2j/pdb
• Descriptor: DNA-binding protein SATB1 (2 entities in total)
• Functional Keywords: dna binding protein
• Biological source: Mus musculus (mouse)
• Cellular location: Nucleus: Q60611
• Total number of polymer chains: 4
• Total formula weight: 80932.57

Authors

Wang, Z.,Long, J.,Yang, X.,Shen, Y. (deposition date: 2014-04-08, release date: 2015-03-11, Last modification date: 2024-03-20)

Primary citation

Wang, Z.,Yang, X.,Guo, S.,Yang, Y.,Su, X.C.,Shen, Y.,Long, J.
Crystal structure of the ubiquitin-like domain-CUT repeat-like tandem of special AT-rich sequence binding protein 1 (SATB1) reveals a coordinating DNA-binding mechanism.
J.Biol.Chem., 289:27376-27385, 2014

PubMed Abstract: SATB1 is essential for T-cell development and growth and metastasis of multitype tumors and acts as a global chromatin organizer and gene expression regulator. The DNA binding ability of SATB1 plays vital roles in its various biological functions. We report the crystal structure of the N-terminal module of SATB1. Interestingly, this module contains a ubiquitin-like domain (ULD) and a CUT repeat-like (CUTL) domain (ULD-CUTL tandem). Detailed biochemical experiments indicate that the N terminus of SATB1 (residues 1-248, SATB1((1-248))), including the extreme 70 N-terminal amino acids, and the ULD-CUTL tandem bind specifically to DNA targets. Our results show that the DNA binding ability of full-length SATB1 requires the contribution of the CUTL domain, as well as the CUT1-CUT2 tandem domain and the homeodomain. These findings may reveal a multiple-domain-coordinated mechanism whereby SATB1 recognizes DNA targets.

PubMed: 25124042
DOI: 10.1074/jbc.M114.562314

Experimental method

X-RAY DIFFRACTION (2.603 Å)