1Y96

crystal structure of the Gemin6/Gemin7 heterodimer from the human SMN complex

Summary for 1Y96

• Entry DOI: 10.2210/pdb1y96/pdb
• Descriptor: Gem-associated protein 6, Gem-associated protein 7 (3 entities in total)
• Functional Keywords: sm fold, protein complex, rna binding protein
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus, nucleoplasm: Q8WXD5 Q9H840
• Total number of polymer chains: 4
• Total formula weight: 38868.13

Authors

Ma, Y.,Dostie, J.,Dreyfuss, G.,Van Duyne, G.D. (deposition date: 2004-12-14, release date: 2005-06-21, Last modification date: 2024-02-14)

Primary citation

Ma, Y.,Dostie, J.,Dreyfuss, G.,Van Duyne, G.D.
The Gemin6-Gemin7 Heterodimer from the Survival of Motor Neurons Complex Has an Sm Protein-like Structure.
Structure, 13:883-892, 2005

PubMed Abstract: The survival of motor neurons (SMN) protein, product of the disease gene of the common neurodegenerative disease spinal muscular atrophy, is part of the large multiprotein "SMN complex." The SMN complex functions as an assembly machine for small nuclear ribonucleoproteins (snRNPs)-the major components of the spliceosome. Here, we report the crystal structure of two components of the human SMN complex, Gemin6 and Gemin7. Although Gemin6 and Gemin7 have no significant sequence similarity with Sm proteins, both adopt canonical Sm folds. Moreover, Gemin6 and Gemin7 exist as a heterodimer, and interact with each other via an interface similar to that which mediates interactions among the Sm proteins. Together with binding experiments that show that the Gemin6/Gemin7 complex binds to Sm proteins, these findings provide a framework for considering how the SMN complex, with Gemin6 and Gemin7 as tools, might organize Sm proteins for formation of Sm rings on snRNA targets.

PubMed: 15939020
DOI: 10.1016/j.str.2005.03.014

Experimental method

X-RAY DIFFRACTION (2.002 Å)