PDBsum entry: 1otr

Cell cycle

PDB-id: 1otr

Contents

Description

Header details

Header records

References

PROCHECK

Protein chains

49 a.a.

76 a.a. *

* Residue conservation analysis

Tools

Clefts Calculation

PDB id:

1otr

Name:

Cell cycle

Title:

Solution structure of a cue-ubiquitin complex

Structure:

Protein cue2. Chain: a. Fragment: amino-terminal cue domain, residues 6-54. Synonym: hypothetical 50.9 kd protein in bud2-mif2 intergenic region. Hypothetical protein ykl090w. Engineered: yes. Ubiquitin. Chain: b. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: cue2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Gene: ubi1.

UniProt:

Chain A: P36075 (CUE2_YEAST)

Seq:
Struc:
	Seq:	443 a.a.
	Struc:	49 a.a.

Chain B: P61864 (UBIQ_YEAST)

Seq:

76 a.a.

Struc:

76 a.a.

Key:	PfamA domain
Secondary structure	CATH domain

Resolution:

not givenÅ

NMR structure:

20 models

Authors:

R.S.Kang,C.M.Daniels,W.J.Salerno,I.Radhakrishnan

Key ref:

R.S.Kang et al. (2003). Solution structure of a CUE-ubiquitin complex reveals a conserved mode of ubiquitin binding.. Cell, 113, 621-630. [PubMed id: 12787503] [DOI: 10.1016/S0092-8674(03)00362-3]

Date:

22-Mar-03

Release date:

24-Jun-03

Quick_links

Procheck

Clefts

Surface

Key reference

DOI no: 10.1016/S0092-8674(03)00362-3

Cell 113:621-630 (2003)

PubMed id: 12787503

Solution structure of a CUE-ubiquitin complex reveals a conserved mode of ubiquitin binding.

R.S.Kang, C.M.Daniels, S.A.Francis, S.C.Shih, W.J.Salerno, L.Hicke, I.Radhakrishnan.

ABSTRACT

Monoubiquitination serves as a regulatory signal in a variety of cellular processes. Monoubiquitin signals are transmitted by binding to a small but rapidly expanding class of ubiquitin binding motifs. Several of these motifs, including the CUE domain, also promote intramolecular monoubiquitination. The solution structure of a CUE domain of the yeast Cue2 protein in complex with ubiquitin reveals intermolecular interactions involving conserved hydrophobic surfaces, including the Leu8-Ile44-Val70 patch on ubiquitin. The contact surface extends beyond this patch and encompasses Lys48, a site of polyubiquitin chain formation. This suggests an occlusion mechanism for inhibiting polyubiquitin chain formation during monoubiquitin signaling. The CUE domain shares a similar overall architecture with the UBA domain, which also contains a conserved hydrophobic patch. Comparative modeling suggests that the UBA domain interacts analogously with ubiquitin. The structure of the CUE-ubiquitin complex may thus serve as a paradigm for ubiquitin recognition and signaling by ubiquitin binding proteins.

Selected figure(s)

Figure 4.
Figure 4. Solution Structure of the CUE2-1-Ubiquitin ComplexStereo views of (A) the C^α trace of a best-fit superposition of backbone atoms in well-ordered regions (residues 9–47 of CUE2-1 and 1–72 of ubiquitin) of the ensemble of 20 NMR structures and (B) a ribbon diagram of a representative structure from the ensemble. CUE2-1 is colored in purple, and ubiquitin is shown in green.

Figure 6.
Figure 6. Intermolecular Interactions and Contributions to the Overall Stability of the CUE2-1-Ubiquitin Complex(A) A view of the molecular surface of CUE2-1, color-coded according to curvature (gray, concave; white, planar; and magenta, convex), shown along with the interacting side chains (blue) of ubiquitin. The backbones of the interacting ubiquitin residues are shown in a worm representation (yellow).(B) Binding of GST, GST-ubiquitin, or GST-ubiquitin mutants to His[6]-CUE2-1. Bound proteins were resolved via SDS-PAGE and analyzed by Coomassie staining (top). The bottom shows the amount of GST or GST-ubiquitin used in these assays.

The above figures are reprinted by permission from Cell Press: Cell (2003, 113, 621-630) copyright 2003.

Figures were selected by an automated process.