5TEF

Crystal structure of Gemin5 WD40 repeats in complex with m7GpppG

Summary for 5TEF

• Entry DOI: 10.2210/pdb5tef/pdb
• Related: 5tee
• Descriptor: Gem-associated protein 5, 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE-5'-GUANOSINE, GLYCEROL, ... (5 entities in total)
• Functional Keywords: structural genomics, structural genomics consortium, sgc, splicing
• Biological source: Homo sapiens (Human)
• Cellular location: Nucleus, nucleoplasm : Q8TEQ6
• Total number of polymer chains: 1
• Total formula weight: 85249.92

Authors

Chao, X.,Tempel, W.,Bian, C.,He, H.,Cerovina, T.,Seitova, A.,Bountra, C.,Arrowsmith, C.H.,Edwards, A.M.,Min, J.,Structural Genomics Consortium (SGC) (deposition date: 2016-09-21, release date: 2016-10-19, Last modification date: 2024-04-03)

Primary citation

Xu, C.,Ishikawa, H.,Izumikawa, K.,Li, L.,He, H.,Nobe, Y.,Yamauchi, Y.,Shahjee, H.M.,Wu, X.H.,Yu, Y.T.,Isobe, T.,Takahashi, N.,Min, J.
Structural insights into Gemin5-guided selection of pre-snRNAs for snRNP assembly.
Genes Dev., 30:2376-2390, 2016

PubMed Abstract: In cytoplasm, the survival of motor neuron (SMN) complex delivers pre-small nuclear RNAs (pre-snRNAs) to the heptameric Sm ring for the assembly of the ring complex on pre-snRNAs at the conserved Sm site [A(U)G]. Gemin5, a WD40 protein component of the SMN complex, is responsible for recognizing pre-snRNAs. In addition, Gemin5 has been reported to specifically bind to the mG cap. In this study, we show that the WD40 domain of Gemin5 is both necessary and sufficient for binding the Sm site of pre-snRNAs by isothermal titration calorimetry (ITC) and mutagenesis assays. We further determined the crystal structures of the WD40 domain of Gemin5 in complex with the Sm site or mG cap of pre-snRNA, which reveal that the WD40 domain of Gemin5 recognizes the Sm site and mG cap of pre-snRNAs via two distinct binding sites by respective base-specific interactions. In addition, we also uncovered a novel role of Gemin5 in escorting the truncated forms of U1 pre-snRNAs for proper disposal. Overall, the elucidated Gemin5 structures will contribute to a better understanding of Gemin5 in small nuclear ribonucleic protein (snRNP) biogenesis as well as, potentially, other cellular activities.

PubMed: 27881600
DOI: 10.1101/gad.288340.116

Experimental method

X-RAY DIFFRACTION (1.95 Å)