4V98

The 8S snRNP Assembly Intermediate

This is a non-PDB format compatible entry.

Summary for 4V98

• Entry DOI: 10.2210/pdb4v98/pdb
• Descriptor: Small nuclear ribonucleoprotein Sm D1, Small nuclear ribonucleoprotein Sm D2, Small nuclear ribonucleoprotein E, ... (9 entities in total)
• Functional Keywords: complex, assembly machinery, splicing
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm, cytosol : P62314 P62316 P62304 P62306 P62308; Cytoplasm : Q9VV74 Q9VVX0
• Total number of polymer chains: 160
• Total formula weight: 2376864.29

Authors

Grimm, C.,Pelz, J.P.,Schindelin, H.,Diederichs, K.,Kuper, J.,Kisker, C. (deposition date: 2012-05-15, release date: 2014-07-09, Last modification date: 2023-09-20)

Primary citation

Grimm, C.,Chari, A.,Pelz, J.P.,Kuper, J.,Kisker, C.,Diederichs, K.,Stark, H.,Schindelin, H.,Fischer, U.
Structural Basis of Assembly Chaperone- Mediated snRNP Formation.
Mol.Cell, 49:692-703, 2013

PubMed Abstract: Small nuclear ribonucleoproteins (snRNPs) represent key constituents of major and minor spliceosomes. snRNPs contain a common core, composed of seven Sm proteins bound to snRNA, which forms in a step-wise and factor-mediated reaction. The assembly chaperone pICln initially mediates the formation of an otherwise unstable pentameric Sm protein unit. This so-called 6S complex docks subsequently onto the SMN complex, which removes pICln and enables the transfer of pre-assembled Sm proteins onto snRNA. X-ray crystallography and electron microscopy was used to investigate the structural basis of snRNP assembly. The 6S complex structure identifies pICln as an Sm protein mimic, which enables the topological organization of the Sm pentamer in a closed ring. A second structure of 6S bound to the SMN complex components SMN and Gemin2 uncovers a plausible mechanism of pICln elimination and Sm protein activation for snRNA binding. Our studies reveal how assembly factors facilitate formation of RNA-protein complexes in vivo.

PubMed: 23333303
DOI: 10.1016/j.molcel.2012.12.009

Experimental method

X-RAY DIFFRACTION (3.1 Å)