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4WJV

Crystal structure of Rsa4 in complex with the Nsa2 binding peptide

Summary for 4WJV
Entry DOI10.2210/pdb4wjv/pdb
Related4WJU
Related PRD IDPRD_900001
DescriptorRibosome assembly protein 4, Maltose-binding periplasmic protein, Ribosome biogenesis protein NSA2, ... (5 entities in total)
Functional Keywordsribosome biogenesis ribosome assembly, protein binding
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
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Total number of polymer chains12
Total formula weight348677.54
Authors
Holdermann, I.,Paternoga, H.,Bassler, J.,Hurt, E.,Sinning, I. (deposition date: 2014-10-01, release date: 2014-11-19, Last modification date: 2024-01-10)
Primary citationBaler, 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: 25404745
DOI: 10.1083/jcb.201408111
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.2 Å)
Structure validation

229380

건을2024-12-25부터공개중

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