5BJR

Crystal structure of the N-terminal RRM domain from MEC-8

Summary for 5BJR

• Entry DOI: 10.2210/pdb5bjr/pdb
• Descriptor: Mec-8 protein, AMMONIUM ION (3 entities in total)
• Functional Keywords: alternative splicing, mrna, rna-binding protein, splicing
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 2
• Total formula weight: 20686.06

Authors

Soufari, H.,Mackereth, C.D. (deposition date: 2016-10-22, release date: 2017-01-11, Last modification date: 2024-01-10)

Primary citation

Soufari, H.,Mackereth, C.D.
Conserved binding of GCAC motifs by MEC-8, couch potato, and the RBPMS protein family.
RNA, 23:308-316, 2017

PubMed Abstract: Precise regulation of mRNA processing, translation, localization, and stability relies on specific interactions with RNA-binding proteins whose biological function and target preference are dictated by their preferred RNA motifs. The RBPMS family of RNA-binding proteins is defined by a conserved RNA recognition motif (RRM) domain found in metazoan RBPMS/Hermes and RBPMS2, couch potato, and MEC-8 from In order to determine the parameters of RNA sequence recognition by the RBPMS family, we have first used the N-terminal domain from MEC-8 in binding assays and have demonstrated a preference for two GCAC motifs optimally separated by >6 nucleotides (nt). We have also determined the crystal structure of the dimeric N-terminal RRM domain from MEC-8 in the unbound form, and in complex with an oligonucleotide harboring two copies of the optimal GCAC motif. The atomic details reveal the molecular network that provides specificity to all four bases in the motif, including multiple hydrogen bonds to the initial guanine. Further studies with human RBPMS, as well as couch potato, confirm a general preference for this double GCAC motif by other members of the protein family and the presence of this motif in known targets.

PubMed: 28003515
DOI: 10.1261/rna.059733.116

Experimental method

X-RAY DIFFRACTION (2.6 Å)