5O9E

Crystal structure of the Imp4-Mpp10 complex from Chaetomium thermophilum

Summary for 5O9E

• Entry DOI: 10.2210/pdb5o9e/pdb
• Descriptor: Putative U3 small nucleolar ribonucleoprotein, Putative U3 small nucleolar ribonucleoprotein protein, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: ribosome biogenesis, ribosome, brix
• Biological source: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719); More
• Total number of polymer chains: 2
• Total formula weight: 37649.75

Authors

Kharde, S.,Ahmed, Y.L.,Sinning, I. (deposition date: 2017-06-19, release date: 2017-08-30, Last modification date: 2024-01-17)

Primary citation

Sa-Moura, B.,Kornprobst, M.,Kharde, S.,Ahmed, Y.L.,Stier, G.,Kunze, R.,Sinning, I.,Hurt, E.
Mpp10 represents a platform for the interaction of multiple factors within the 90S pre-ribosome.
PLoS ONE, 12:e0183272-e0183272, 2017

PubMed Abstract: In eukaryotes, ribosome assembly is a highly complex process that involves more than 200 assembly factors that ensure the folding, modification and processing of the different rRNA species as well as the timely association of ribosomal proteins. One of these factors, Mpp10 associates with Imp3 and Imp4 to form a complex that is essential for the normal production of the 18S rRNA. Here we report the crystal structure of a complex between Imp4 and a short helical element of Mpp10 to a resolution of 1.88 Å. Furthermore, we extend the interaction network of Mpp10 and characterize two novel interactions. Mpp10 is able to bind the ribosome biogenesis factor Utp3/Sas10 through two conserved motifs in its N-terminal region. In addition, Mpp10 interacts with the ribosomal protein S5/uS7 using a short stretch within an acidic loop region. Thus, our findings reveal that Mpp10 provides a platform for the simultaneous interaction with multiple proteins in the 90S pre-ribosome.

PubMed: 28813493
DOI: 10.1371/journal.pone.0183272

Experimental method

X-RAY DIFFRACTION (1.884 Å)