3GYP: Rtt106p

Rtt106p is a Saccharomyces cerevisiae histone chaperone with roles in heterochromatin silencing and nucleosome assembly. The molecular mechanism by which Rtt106p engages in chromatin dynamics remains unclear. Here, we report the 2.5 A crystal structure of the core domain of Rtt106p, which adopts an unusual "double pleckstrin homology" domain architecture that represents a novel structural mode for histone chaperones. A histone H3-H4-binding region and a novel double-stranded DNA-binding region have been identified. Mutagenesis studies reveal that the histone and DNA binding activities of Rtt106p are involved in Sir protein-mediated heterochromatin formation. Our results uncover the structural basis of the diverse functions of Rtt106p and provide new insights into its cellular roles.
PDB ID: 3GYPDownload
MMDB ID: 78550
PDB Deposition Date: 2009/4/4
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 2.406  Å
Source Organism:
Similar Structures:
Biological Unit for 3GYP: monomeric; determined by author and by software (PISA)
Molecular Components in 3GYP
Label Count Molecule
Protein (1 molecule)
Histone Chaperone Rtt106(Gene symbol: RTT106)
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB