4WJS
Crystal structure of Rsa4 from Chaetomium thermophilum
Summary for 4WJS
Entry DOI | 10.2210/pdb4wjs/pdb |
Descriptor | Rsa4 (2 entities in total) |
Functional Keywords | ribosome assembly, ribosome biogenesis, biosynthetic protein |
Biological source | Chaetomium thermophilum |
Cellular location | Nucleus, nucleolus : G0SC29 |
Total number of polymer chains | 1 |
Total formula weight | 53999.56 |
Authors | Holdermann, I.,Bassler, J.,Hurt, E.,Sinning, I. (deposition date: 2014-10-01, release date: 2014-11-19, Last modification date: 2024-01-10) |
Primary citation | Baler, J.,Paternoga, H.,Holdermann, I.,Thoms, M.,Granneman, S.,Barrio-Garcia, C.,Nyarko, A.,Stier, G.,Clark, S.A.,Schraivogel, D.,Kallas, M.,Beckmann, R.,Tollervey, D.,Barbar, E.,Sinning, I.,Hurt, E. A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation. J.Cell Biol., 207:481-498, 2014 Cited by PubMed Abstract: Eukaryotic ribosome biogenesis involves ∼200 assembly factors, but how these contribute to ribosome maturation is poorly understood. Here, we identify a network of factors on the nascent 60S subunit that actively remodels preribosome structure. At its hub is Rsa4, a direct substrate of the force-generating ATPase Rea1. We show that Rsa4 is connected to the central protuberance by binding to Rpl5 and to ribosomal RNA (rRNA) helix 89 of the nascent peptidyl transferase center (PTC) through Nsa2. Importantly, Nsa2 binds to helix 89 before relocation of helix 89 to the PTC. Structure-based mutations of these factors reveal the functional importance of their interactions for ribosome assembly. Thus, Rsa4 is held tightly in the preribosome and can serve as a "distribution box," transmitting remodeling energy from Rea1 into the developing ribosome. We suggest that a relay-like factor network coupled to a mechano-enzyme is strategically positioned to relocate rRNA elements during ribosome maturation. PubMed: 25404745DOI: 10.1083/jcb.201408111 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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