PDBsum entry 1p27

RNA binding protein

PDB id: 1p27

Contents

Protein chains

144 a.a. *

92 a.a. *

Waters ×100

* Residue conservation analysis

PDB id:

1p27

Name:

RNA binding protein

Title:

Crystal structure of the human y14/magoh complex

Structure:

Mago nashi protein homolog. Chain: a, c. Engineered: yes. RNA-binding protein 8a. Chain: b, d. Synonym: RNA binding motif protein 8a, ribonucleoprotein rbm8a, RNA- binding protein y14, binder of ovca1- 1, bov-1. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: magoh. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Gene: rbm8a or rbm8.

Biol. unit:

Tetramer (from PQS)

Resolution:

2.00Å R-factor: 0.222 R-free: 0.268

Authors:

C.K.Lau,M.D.Diem,G.Dreyfuss,G.D.Van Duyne

Key ref:

C.K.Lau et al. (2003). Structure of the Y14-Magoh core of the exon junction complex. Curr Biol, 13, 933-941. PubMed id: 12781131 DOI: 10.1016/S0960-9822(03)00328-2

Date:

14-Apr-03 Release date: 19-Aug-03

Protein chains

P61326  (MGN_HUMAN) -  Protein mago nashi homolog from Homo sapiens

Seq: 146 a.a.

Struc: 144 a.a.

Protein chains

Q9Y5S9  (RBM8A_HUMAN) -  RNA-binding protein 8A from Homo sapiens

Seq: 174 a.a.

Struc: 92 a.a.

Enzyme reactions

• Enzyme class: Chains A, B, C, D: E.C.?

DOI no: 10.1016/S0960-9822(03)00328-2

Curr Biol 13:933-941 (2003)

PubMed id: 12781131

Structure of the Y14-Magoh core of the exon junction complex.

C.K.Lau, M.D.Diem, G.Dreyfuss, G.D.Van Duyne.

ABSTRACT

BACKGROUND: Splicing of pre-mRNA in eukaryotes imprints the resulting mRNA with a specific multiprotein complex, the exon-exon junction complex (EJC), at the sites of intron removal. The proteins of the EJC, Y14, Magoh, Aly/REF, RNPS1, Srm160, and Upf3, play critical roles in postsplicing processing, including nuclear export and cytoplasmic localization of the mRNA, and the nonsense-mediated mRNA decay (NMD) surveillance process. Y14 and Magoh are of particular interest because they remain associated with the mRNA in the same position after its export to the cytoplasm and require translation of the mRNA for removal. This tenacious, persistent, splicing-dependent, yet RNA sequence-independent, association suggests an important signaling function and must require distinct structural features for these proteins. RESULTS: We describe the high-resolution structure and biochemical properties of the highly conserved human Y14 and Magoh proteins. Magoh has an unusual structure comprised of an extremely flat, six-stranded anti-parallel beta sheet packed against two helices. Surprisingly, Magoh binds with high affinity to the RNP motif RNA binding domain (RBD) of Y14 and completely masks its RNA binding surface. CONCLUSIONS: The structure and properties of the Y14-Magoh complex suggest how the pre-mRNA splicing machinery might control the formation of a stable EJC-mRNA complex at splice junctions.

Selected figure(s)

Figure 2.
Figure 2. Structure of Human Magoh(A) Alignment of a diverse subset of known Magoh sequences. The shaded regions indicate ≥80% sequence identity. Secondary structure assignments are shown above the alignments, and residues contacting Y14 (< 3.8 Å) are marked with an asterisk. Hs, human; Dm, D. melanogaster; Ce, C. elegans; At, A. thaliana; Sp, S. pombe.(B) A ribbon diagram of Magoh as seen bound to Y14.(C) σ[A]-weighted 2Fo-Fc electron density for the refined structure at 2 Å resolution, contoured at 1.4 σ. The orientation of the indicated β strands is the same as that shown in (B).The molecular drawings in Figure 2, Figure 3, Figure 4, Figure 5 and Figure 6 were prepared with PYMOL [46].

Figure 3.
Figure 3. Sequence Conservation Mapped onto the Magoh StructureLight-blue residues correspond to the shaded regions in Figure 2A (≥80% identity), and dark-blue residues are less conserved.(A) Same orientation as in Figures 2B and 2C.(B) View from the opposite face, showing the concave surface formed by the β sheet extension.

The above figures are reprinted by permission from Cell Press: Curr Biol (2003, 13, 933-941) copyright 2003.

Figures were selected by an automated process.