4BSZ

Crystal Structure of the Yeast Ribosomal Protein Rps3 in Complex with its Chaperone Yar1

Summary for 4BSZ

• Entry DOI: 10.2210/pdb4bsz/pdb
• Descriptor: 40S RIBOSOMAL PROTEIN S3, ANKYRIN REPEAT-CONTAINING PROTEIN YAR1 (2 entities in total)
• Functional Keywords: rna binding protein
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Cellular location: Cytoplasm (By similarity): P05750
• Total number of polymer chains: 2
• Total formula weight: 49565.99

Authors

Holzer, S.,Ban, N.,Klinge, S. (deposition date: 2013-06-12, release date: 2013-09-04, Last modification date: 2023-12-20)

Primary citation

Holzer, S.,Ban, N.,Klinge, S.
Crystal Structure of the Yeast Ribosomal Protein Rps3 in Complex with its Chaperone Yar1
J.Mol.Biol., 425:4154-, 2013

PubMed Abstract: Eukaryotic ribosome assembly involves a plethora of factors, which ensure that a correctly folded ribosome contains all ribosomal protein components. Among these assembly factors, Yar1 has recently emerged as a molecular chaperone for ribosomal protein rpS3 of the small ribosomal subunit (40S) in yeast. In complex with its chaperone, rpS3 is imported into the nucleus and protected from aggregation. How rpS3 and other ribosomal proteins are initially sequestered and subsequently integrated into pre-ribosomal particles is currently poorly understood. Here, we present the crystal structure of yeast rpS3 in complex with its chaperone Yar1 at 2.8Å resolution. The crystal structure rationalizes how Yar1 can protect rpS3 from aggregation while facilitating nuclear import and suggests a mechanism for a stepwise exchange of molecular partners that ribosomal proteins interact with during ribosome assembly.

PubMed: 24021814
DOI: 10.1016/J.JMB.2013.08.022

Experimental method

X-RAY DIFFRACTION (2.842 Å)