3GYP

Rtt106p

Summary for 3GYP

• Entry DOI: 10.2210/pdb3gyp/pdb
• Related: 3GYO
• Descriptor: Histone chaperone RTT106, BETA-MERCAPTOETHANOL, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: histone chaperone, chaperone, chromosomal protein, nucleus, phosphoprotein, transcription, transcription regulation, transposition
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Nucleus: P40161
• Total number of polymer chains: 1
• Total formula weight: 29920.75

Authors

Liu, Y.,Huang, H.,Shi, Y.,Teng, M. (deposition date: 2009-04-04, release date: 2009-12-08, Last modification date: 2024-05-29)

Primary citation

Liu, Y.,Huang, H.,Zhou, B.O.,Wang, S.S.,Hu, Y.,Li, X.,Liu, J.,Zang, J.,Niu, L.,Wu, J.,Zhou, J.Q.,Teng, M.,Shi, Y.
Structural analysis of Rtt106p reveals a DNA-binding role required for heterochromatin silencing
J.Biol.Chem., 285:4251-4262, 2010

PubMed Abstract: 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.

PubMed: 20007951
DOI: 10.1074/jbc.M109.055996

Experimental method

X-RAY DIFFRACTION (2.406 Å)