EMD-40780

Single-particle
3.38 Å
EMD-40780 Deposition: 14/05/2023
Map released: 25/09/2024
Last modified: 02/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-40780

Cryo-EM structure of the human cap binding complex (CBC)

EMD-40780

Single-particle
3.38 Å
EMD-40780 Deposition: 14/05/2023
Map released: 25/09/2024
Last modified: 02/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Homo sapiens
Sample: Cryo-EM structure of an mRNA export factor
Fitted models: 8suy (Avg. Q-score: 0.43)

Deposition Authors: Xie Y , Clarke BP , Ren Y
Cryo-EM structure of the CBC-ALYREF complex.
Clarke BP , Angelos AE, Mei M, Hill PS , Xie Y , Ren Y
(2024) eLife , 12
PUBMED: 39282949
DOI: doi:10.7554/eLife.91432
ISSN: 2050-084X
Abstract:
In eukaryotes, RNAs transcribed by RNA Pol II are modified at the 5' end with a 7-methylguanosine (m7G) cap, which is recognized by the nuclear cap binding complex (CBC). The CBC plays multiple important roles in mRNA metabolism, including transcription, splicing, polyadenylation, and export. It promotes mRNA export through direct interaction with a key mRNA export factor, ALYREF, which in turn links the TRanscription and EXport (TREX) complex to the 5' end of mRNA. However, the molecular mechanism for CBC-mediated recruitment of the mRNA export machinery is not well understood. Here, we present the first structure of the CBC in complex with an mRNA export factor, ALYREF. The cryo-EM structure of CBC-ALYREF reveals that the RRM domain of ALYREF makes direct contact with both the NCBP1 and NCBP2 subunits of the CBC. Comparing CBC-ALYREF with other cellular complexes containing CBC and/or ALYREF components provides insights into the coordinated events during mRNA transcription, splicing, and export.