3TUO: Crystal Structure Of N-terminal Domain Of Dna-binding Protein Satb1

Citation:
Abstract
Special AT-rich sequence-binding protein 1 (SATB1) is a global chromatin organizer and gene expression regulator essential for T-cell development and breast cancer tumor growth and metastasis. The oligomerization of the N-terminal domain of SATB1 is critical for its biological function. We determined the crystal structure of the N-terminal domain of SATB1. Surprisingly, this domain resembles a ubiquitin domain instead of the previously proposed PDZ domain. Our results also reveal that SATB1 can form a tetramer through its N-terminal domain. The tetramerization of SATB1 plays an essential role in its binding to highly specialized DNA sequences. Furthermore, isothermal titration calorimetry results indicate that the SATB1 tetramer can bind simultaneously to two DNA targets. Based on these results, we propose a molecular model whereby SATB1 regulates the expression of multiple genes both locally and at a distance.
PDB ID: 3TUODownload
MMDB ID: 96909
PDB Deposition Date: 2011/9/17
Updated in MMDB: 2013/06
Experimental Method:
x-ray diffraction
Resolution: 1.7  Å
Source Organism:
Similar Structures:
Biological Unit for 3TUO: tetrameric; determined by author and by software (PISA)
Molecular Components in 3TUO
Label Count Molecule
Proteins (4 molecules)
4
DNA-binding Protein Satb1(Gene symbol: SATB1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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