PDBsum entry 1jmt

RNA binding protein

PDB id: 1jmt

Contents

Protein chains

98 a.a. *

23 a.a. *

Ligands

HEZ ×2

Waters ×118

* Residue conservation analysis

PDB id:

1jmt

Name:

RNA binding protein

Title:

X-ray structure of a core u2af65/u2af35 heterodimer

Structure:

Splicing factor u2af 35 kda subunit. Chain: a. Synonym: u2 snrnp auxiliary factor small subunit. Engineered: yes. Mutation: yes. Splicing factor u2af 65 kda subunit. Chain: b. Synonym: u2 snrnp auxiliary factor large subunit. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

Biol. unit:

Octamer (from PQS)

Resolution:

2.20Å R-factor: 0.226 R-free: 0.238

Authors:

C.L.Kielkopf,N.A.Rodionova,M.R.Green,S.K.Burley

Key ref:

C.L.Kielkopf et al. (2001). A novel peptide recognition mode revealed by the X-ray structure of a core U2AF35/U2AF65 heterodimer. Cell, 106, 595-605. PubMed id: 11551507 DOI: 10.1016/S0092-8674(01)00480-9

Date:

19-Jul-01 Release date: 19-Sep-01

Protein chain

Q01081  (U2AF1_HUMAN) -  Splicing factor U2AF 35 kDa subunit from Homo sapiens

Seq: 240 a.a.

Struc: 98 a.a.*

Protein chain

P26368  (U2AF2_HUMAN) -  Splicing factor U2AF 65 kDa subunit from Homo sapiens

Seq: 475 a.a.

Struc: 23 a.a.

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: Chains A, B: E.C.?

DOI no: 10.1016/S0092-8674(01)00480-9

Cell 106:595-605 (2001)

PubMed id: 11551507

A novel peptide recognition mode revealed by the X-ray structure of a core U2AF35/U2AF65 heterodimer.

C.L.Kielkopf, N.A.Rodionova, M.R.Green, S.K.Burley.

ABSTRACT

U2 auxiliary factor (U2AF) is an essential splicing factor that recognizes the 3' splice site and recruits the U2 snRNP to the branch point. The X-ray structure of the human core U2AF heterodimer, consisting of the U2AF35 central domain and a proline-rich region of U2AF65, has been determined at 2.2 A resolution. The structure reveals a novel protein-protein recognition strategy, in which an atypical RNA recognition motif (RRM) of U2AF35 and the U2AF65 polyproline segment interact via reciprocal "tongue-in-groove" tryptophan residues. Complementary biochemical experiments demonstrate that the core U2AF heterodimer binds RNA, and that the interacting tryptophan side chains are essential for U2AF dimerization. Atypical RRMs in other splicing factors may serve as protein-protein interaction motifs elsewhere during spliceosome assembly.

Selected figure(s)

Figure 1.
Figure 1. Structure of the U2AF^35/U2AF^65 Complex(A) Stereoview of the U2AF^65 proline-rich loop enveloping U2AF^35 Trp134. Density modified, experimental electron density map for residues Trp92p to Pro104p of U2AF^65 contoured at 1σ. The U2AF^65 peptide is shown in pink, or color coded for atom type (yellow, carbon; red, oxygen; and blue, nitrogen) and the U2AF^35 domain is shown in light blue. Six disordered amino acids linking α helix A with the RNP2 β strand 1 are represented with a dashed line. The RNP motifs and α helices A and B are labeled.(B) The U2AF complex viewed along the cylindrical axis of α helix A. A schematic representation of the reciprocal tryptophan binding sites is shown on the left.(C) View of the binary complex perpendicular to the perspective of (B).(D) U2AF^35 β sheet that forms the RNA binding surfaces of canonical RRM-containing proteins

Figure 3.
Figure 3. Reciprocal Tryptophan Recognition within the U2AF HeterodimerStereodrawings of interactions with (A) U2AF^35 Trp134 and (B) U2AF^65 Trp92p

The above figures are reprinted by permission from Cell Press: Cell (2001, 106, 595-605) copyright 2001.

Figures were selected by an automated process.