4EJS

Structure of yeast elongator subcomplex Elp456

Summary for 4EJS

• Entry DOI: 10.2210/pdb4ejs/pdb
• Descriptor: Elongator complex protein 4, Elongator complex protein 5, Elongator complex protein 6, ... (4 entities in total)
• Functional Keywords: elongator subcomplex elp456, reca-atpase-like domain fold, transcription
• Biological source: Saccharomyces cerevisiae (yeast); More
• Cellular location: Cytoplasm: Q02884 P38874 Q04868
• Total number of polymer chains: 3
• Total formula weight: 100754.42

Authors

Lin, Z.,Zhao, W.,Long, J.,Shen, Y. (deposition date: 2012-04-07, release date: 2012-05-02, Last modification date: 2024-03-20)

Primary citation

Lin, Z.,Zhao, W.,Diao, W.,Xie, X.,Wang, Z.,Zhang, J.,Shen, Y.,Long, J.
Crystal structure of elongator subcomplex Elp4-6
J.Biol.Chem., 287:21501-21508, 2012

PubMed Abstract: Elongator is a multiprotein complex composed of two subcomplexes, Elp1-3 and Elp4-6. Elongator is highly conserved between yeast and humans and plays an important role in RNA polymerase II-mediated transcriptional elongation and many other processes, including cytoskeleton organization, exocytosis, and tRNA modification. Here, we determined the crystal structure of the Elp4-6 subcomplex of yeast. The overall structure of Elp4-6 revealed that Elp6 acts as a bridge to assemble Elp4 and Elp5. Detailed structural and sequence analyses revealed that each subunit in the Elp4-6 subcomplex forms a RecA-ATPase-like fold, although it lacks the key sequence signature of ATPases. Site-directed mutagenesis and biochemical analyses indicated that the Elp4-6 subcomplex can assemble into a hexameric ring-shaped structure in vitro and in vivo. Furthermore, GST pulldown assays showed that the ring-shaped assembly of the Elp4-6 subcomplex is important for its specific histone H3 binding. Our results may shed light on the substrate recognition and assembly of the holo-Elongator complex.

PubMed: 22556426
DOI: 10.1074/jbc.M112.341560

Experimental method

X-RAY DIFFRACTION (2.606 Å)