PDBsum entry 4cio

RNA binding protein/RNA

PDB id: 4cio

Contents

Protein chain

97 a.a.

DNA/RNA

PDB id:

4cio

Name:

RNA binding protein/RNA

Title:

Rrm domain from c. Elegans sup-12 bound to ggugugc RNA

Structure:

Protein sup-12, isoform a. Chain: a. Fragment: rrm domain, residues 28-121. Synonym: sup-12. Engineered: yes. 5'-r( Gp Gp Up Gp Up Gp Cp)-3'. Chain: b. Fragment: sup-12 binding motif. Engineered: yes.

Source:

Caenorhabditis elegans. Organism_taxid: 6239. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: plysy. Synthetic: yes. Organism_taxid: 6239

NMR struc:

15 models

Authors:

S.Amrane,C.D.Mackereth

Key ref:

S.Amrane et al. (2014). Backbone-independent nucleic acid binding by splicing factor SUP-12 reveals key aspects of molecular recognition. Nat Commun, 5, 4595. PubMed id: 25183497 DOI: 10.1038/ncomms5595

Date:

12-Dec-13 Release date: 03-Sep-14

Protein chain

O45189  (O45189_CAEEL) -  RRM domain-containing protein from Caenorhabditis elegans

Seq: 248 a.a.

Struc: 97 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DNA/RNA chain

G-G-U-G-U-G-C 7 bases

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1038/ncomms5595

Nat Commun 5:4595 (2014)

PubMed id: 25183497

Backbone-independent nucleic acid binding by splicing factor SUP-12 reveals key aspects of molecular recognition.

S.Amrane, K.Rebora, I.Zniber, D.Dupuy, C.D.Mackereth.

ABSTRACT

Cellular differentiation is frequently accompanied by alternative splicing, enabled by the expression of tissue-specific factors which bind to pre-mRNAs and regulate exon choice. During Caenorhabditis elegans development, muscle-specific expression of the splicing factor SUP-12, together with a member of the Fox-1 family of splicing proteins, generates a functionally distinct isoform of the fibroblast growth factor receptor EGL-15. Using a combination of NMR spectroscopy and isothermal titration calorimetry, we determined the mode of nucleic acid binding by the RNA recognition motif domain of SUP-12. The calculated structures provide the first atomic details of RNA and DNA binding by the family of proteins that include SUP-12, RBM24, RBM38/RNPC1, SEB-4 and XSeb4R. This information was further used to design strategic mutations to probe the interaction with ASD-1 and to quantitatively perturb splicing in vivo.