4QMF

Structure of the Krr1 and Faf1 complex from Saccharomyces cerevisiae

Summary for 4QMF

• Entry DOI: 10.2210/pdb4qmf/pdb
• Descriptor: KRR1 small subunit processome component, Protein FAF1 (3 entities in total)
• Functional Keywords: protein-protein complex, k-homology domain, ribosome biogenesis, rna binding protein
• Biological source: Saccharomyces cerevisiae (yeast); More
• Cellular location: Nucleus, nucleolus : P25586 P40546
• Total number of polymer chains: 4
• Total formula weight: 55322.47

Authors

Zheng, S.,Ye, K. (deposition date: 2014-06-16, release date: 2014-07-09, Last modification date: 2024-03-20)

Primary citation

Zheng, S.,Lan, P.,Liu, X.,Ye, K.
Interaction between ribosome assembly factors Krr1 and Faf1 is essential for formation of small ribosomal subunit in yeast
J.Biol.Chem., 289:22692-22703, 2014

PubMed Abstract: Ribosome formation in Saccharomyces cerevisiae requires a large number of transiently associated assembly factors that coordinate processing and folding of pre-rRNA and binding of ribosomal proteins. Krr1 and Faf1 are two interacting proteins present in early 90 S precursor particles of the small ribosomal subunit. Here, we determined a co-crystal structure of the core domain of Krr1 bound to a 19-residue fragment of Faf1 at 2.8 Å resolution. The structure reveals that Krr1 consists of two packed K homology (KH) domains, KH1 and KH2, and resembles archaeal Dim2-like proteins. We show that KH1 is a divergent KH domain that lacks the RNA-binding GXXG motif and is involved in binding another assembly factor, Kri1. KH2 contains a canonical RNA-binding surface and additionally associates with an α-helix of Faf1. Specific disruption of the Krr1-Faf1 interaction impaired early 18 S rRNA processing at sites A0, A1, and A2 and caused cell lethality, but it did not prevent incorporation of the two proteins into pre-ribosomes. The Krr1-Faf1 interaction likely maintains a critical conformation of 90 S pre-ribosomes required for pre-rRNA processing. Our results illustrate the versatility of KH domains in protein interaction and provide insight into the role of Krr1-Faf1 interaction in ribosome biogenesis.

PubMed: 24990943
DOI: 10.1074/jbc.M114.584490

Experimental method

X-RAY DIFFRACTION (2.804 Å)