PDBsum entry 2mkc

Splicing

PDB id: 2mkc

Contents

Protein chains

118 a.a.

23 a.a.

33 a.a.

PDB id:

2mkc

Name:

Splicing

Title:

Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex

Structure:

U2 snrnp component ist3. Chain: a. Fragment: unp residues 25-138. Synonym: increased sodium tolerance protein 3, u2 snrnp protein snu17. Engineered: yes. Pre-mRNA leakage protein 1. Chain: b. Fragment: unp residues 22-42.

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: ist3, snu17, yib5w, yir005w. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: pml1, ylr016c, l1591. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

P.Wysoczanski,C.Schneider,S.Xiang,F.Munari,S.Trowitzsch,M.C.Wahl, R.Luhrmann,S.Becker,M.Zweckstetter

Key ref:

P.Wysoczański et al. (2014). Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Nat Struct Biol, 21, 911-918. PubMed id: 25218446 DOI: 10.1038/nsmb.2889

Date:

04-Feb-14 Release date: 03-Sep-14

Protein chain

P40565  (IST3_YEAST) -  U2 snRNP component IST3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 148 a.a.

Struc: 118 a.a.*

Protein chain

Q07930  (PML1_YEAST) -  Pre-mRNA leakage protein 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 204 a.a.

Struc: 23 a.a.*

Protein chain

P46947  (CWC26_YEAST) -  Pre-mRNA-splicing factor CWC26 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 266 a.a.

Struc: 33 a.a.*

* PDB and UniProt seqs differ at 8 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, B, C: E.C.?

DOI no: 10.1038/nsmb.2889

Nat Struct Biol 21:911-918 (2014)

PubMed id: 25218446

Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex.

P.Wysoczański, C.Schneider, S.Xiang, F.Munari, S.Trowitzsch, M.C.Wahl, R.Lührmann, S.Becker, M.Zweckstetter.

ABSTRACT

The precursor mRNA (pre-mRNA) retention and splicing (RES) complex is a spliceosomal complex that is present in yeast and humans and is important for RNA splicing and retention of unspliced pre-mRNA. Here, we present the solution NMR structure of the RES core complex from Saccharomyces cerevisiae. Complex formation leads to an intricate folding of three components-Snu17p, Bud13p and Pml1p-that stabilizes the RNA-recognition motif (RRM) fold of Snu17p and increases binding affinity in tertiary interactions between the components by more than 100-fold compared to that in binary interactions. RES interacts with pre-mRNA within the spliceosome, and through the assembly of the RES core complex RNA binding efficiency is increased. The three-dimensional structure of the RES core complex highlights the importance of cooperative folding and binding in the functional organization of the spliceosome.