5OO6

Complex of human nuclear cap-binding complex with ARS2 C-terminal peptide

Summary for 5OO6

• Entry DOI: 10.2210/pdb5oo6/pdb
• Descriptor: Nuclear cap-binding protein subunit 1, Nuclear cap-binding protein subunit 2, Serrate RNA effector molecule homolog, ... (4 entities in total)
• Functional Keywords: complex nuclear cap-binding complex m7gtp c-terminal peptide from ars2, nuclear protein
• Biological source: Homo sapiens (Human); More
• Cellular location: Nucleus : Q09161 P52298; Nucleus, nucleoplasm : Q9BXP5
• Total number of polymer chains: 24
• Total formula weight: 911123.26

Authors

Cusack, S.,Schulze, W.M. (deposition date: 2017-08-06, release date: 2017-11-15, Last modification date: 2024-01-17)

Primary citation

Schulze, W.M.,Cusack, S.
Structural basis for mutually exclusive co-transcriptional nuclear cap-binding complexes with either NELF-E or ARS2.
Nat Commun, 8:1302-1302, 2017

PubMed Abstract: Pol II transcribes diverse classes of RNAs that need to be directed into the appropriate nuclear maturation pathway. All nascent Pol II transcripts are 5'-capped and the cap is immediately sequestered by the nuclear cap-binding complex (CBC). Mutually exclusive interactions of CBC with different partner proteins have been implicated in transcript fate determination. Here, we characterise the direct interactions between CBC and NELF-E, a subunit of the negative elongation factor complex, ARS2 and PHAX. Our biochemical and crystal structure results show that the homologous C-terminal peptides of NELF-E and ARS2 bind identically to CBC and in each case the affinity is enhanced when CBC is bound to a cap analogue. Furthermore, whereas PHAX forms a complex with CBC and ARS2, NELF-E binding to CBC is incompatible with PHAX binding. We thus define two mutually exclusive complexes CBC-NELF-E and CBC-ARS2-PHAX, which likely act in respectively earlier and later phases of transcription.

PubMed: 29101316
DOI: 10.1038/s41467-017-01402-w

Experimental method

X-RAY DIFFRACTION (2.8 Å)