4A8J

Crystal Structure of the Elongator subcomplex Elp456

Summary for 4A8J

• Entry DOI: 10.2210/pdb4a8j/pdb
• Descriptor: Elongator complex protein 4, Elongator complex protein 5, Elongator complex protein 6, ... (4 entities in total)
• Functional Keywords: transcription
• Biological source: Saccharomyces cerevisiae S288C; More
• Cellular location: Cytoplasm: Q02884 P38874 Q04868
• Total number of polymer chains: 6
• Total formula weight: 208344.05

Authors

Glatt, S.,Mueller, C.W. (deposition date: 2011-11-21, release date: 2012-02-22, Last modification date: 2024-10-23)

Primary citation

Glatt, S.,Letoquart, J.,Faux, C.,Taylor, N.M.I.,Seraphin, B.,Muller, C.W.
The Elongator Subcomplex Elp456 is a Hexameric Reca-Like ATPase.
Nat.Struct.Mol.Biol., 19:314-, 2012

PubMed Abstract: Elongator was initially described as an RNA polymerase II-associated factor but has since been associated with a broad range of cellular activities. It has also attracted clinical attention because of its role in certain neurodegenerative diseases. Here we describe the crystal structure of the Saccharomyces cerevisiae subcomplex of Elongator proteins 4, 5 and 6 (Elp456). The subunits each show almost identical RecA folds that form a heterohexameric ring-like structure resembling hexameric RecA-like ATPases. This structural finding is supported by different complementary in vitro and in vivo approaches, including the specific binding of the hexameric Elp456 subcomplex to tRNAs in a manner regulated by ATP. Our results support a role of Elongator in tRNA modification, explain the importance of each of the Elp4, Elp5 and Elp6 subunits for complex integrity and suggest a model for the overall architecture of the holo-Elongator complex.

PubMed: 22343726
DOI: 10.1038/NSMB.2234

Experimental method

X-RAY DIFFRACTION (2.1 Å)