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4NUT

Crystal structure of the complex between Snu13p and the PEP domain of Rsa1

Summary for 4NUT
Entry DOI10.2210/pdb4nut/pdb
Descriptor13 kDa ribonucleoprotein-associated protein, Ribosome assembly 1 protein, SULFATE ION, ... (4 entities in total)
Functional Keywordssnornp assembly, rna binding protein
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
More
Cellular locationNucleus, nucleolus: P39990
Nucleus: Q08932
Total number of polymer chains2
Total formula weight20986.38
Authors
Charron, C.,Chagot, M.E.,Manival, X.,Branlant, C.,Charpentier, B. (deposition date: 2013-12-04, release date: 2014-12-10, Last modification date: 2024-03-20)
Primary citationBizarro, J.,Charron, C.,Boulon, S.,Westman, B.,Pradet-Balade, B.,Vandermoere, F.,Chagot, M.E.,Hallais, M.,Ahmad, Y.,Leonhardt, H.,Lamond, A.,Manival, X.,Branlant, C.,Charpentier, B.,Verheggen, C.,Bertrand, E.
Proteomic and 3D structure analyses highlight the C/D box snoRNP assembly mechanism and its control
J.Cell Biol., 207:463-480, 2014
Cited by
PubMed Abstract: In vitro, assembly of box C/D small nucleolar ribonucleoproteins (snoRNPs) involves the sequential recruitment of core proteins to snoRNAs. In vivo, however, assembly factors are required (NUFIP, BCD1, and the HSP90-R2TP complex), and it is unknown whether a similar sequential scheme applies. In this paper, we describe systematic quantitative stable isotope labeling by amino acids in cell culture proteomic experiments and the crystal structure of the core protein Snu13p/15.5K bound to a fragment of the assembly factor Rsa1p/NUFIP. This revealed several unexpected features: (a) the existence of a protein-only pre-snoRNP complex containing five assembly factors and two core proteins, 15.5K and Nop58; (b) the characterization of ZNHIT3, which is present in the protein-only complex but gets released upon binding to C/D snoRNAs; (c) the dynamics of the R2TP complex, which appears to load/unload RuvBL AAA(+) adenosine triphosphatase from pre-snoRNPs; and (d) a potential mechanism for preventing premature activation of snoRNP catalytic activity. These data provide a framework for understanding the assembly of box C/D snoRNPs.
PubMed: 25404746
DOI: 10.1083/jcb.201404160
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.55 Å)
Structure validation

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数据于2025-11-05公开中

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