PDBsum entry 2dwz

Oncoprotein

PDB id: 2dwz

Contents

Protein chains

226 a.a. *

73 a.a. *

Ligands

EPE

Waters ×233

* Residue conservation analysis

PDB id:

2dwz

Name:

Oncoprotein

Title:

Structure of the oncoprotein gankyrin in complex with s6 atpase of the 26s proteasome

Structure:

26s proteasome non-atpase regulatory subunit 10. Chain: a, c. Synonym: 26s proteasome regulatory subunit p28, gankyrin. Engineered: yes. 26s protease regulatory subunit 6b. Chain: b, d. Fragment: c-terminal domain. Synonym: tat-binding protein-7, tbp-7. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562. Rattus norvegicus. Norway rat. Organism_taxid: 10116.

Resolution:

2.40Å R-factor: 0.194 R-free: 0.268

Authors:

B.Padmanabhan,S.Yokoyama,Riken Structural Genomics/proteomics Initiative (Rsgi)

Key ref:

Y.Nakamura et al. (2007). Structure of the oncoprotein gankyrin in complex with S6 ATPase of the 26S proteasome. Structure, 15, 179-189. PubMed id: 17292836 DOI: 10.1016/j.str.2006.11.015

Date:

22-Aug-06 Release date: 28-Aug-07

Protein chains

Q9Z2X2  (PSD10_MOUSE) -  26S proteasome non-ATPase regulatory subunit 10 from Mus musculus

Seq: 231 a.a.

Struc: 226 a.a.*

Protein chains

Q63570  (PRS6B_RAT) -  26S proteasome regulatory subunit 6B from Rattus norvegicus

Seq: 418 a.a.

Struc: 73 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DOI no: 10.1016/j.str.2006.11.015

Structure 15:179-189 (2007)

PubMed id: 17292836

Structure of the oncoprotein gankyrin in complex with S6 ATPase of the 26S proteasome.

Y.Nakamura, K.Nakano, T.Umehara, M.Kimura, Y.Hayashizaki, A.Tanaka, M.Horikoshi, B.Padmanabhan, S.Yokoyama.

ABSTRACT

Gankyrin is an oncoprotein commonly overexpressed in most hepatocellular carcinomas. Gankyrin interacts with S6 ATPase of the 19S regulatory particle of the 26S proteasome and enhances the degradation of the tumor suppressors pRb and p53. Here, we report the structure of gankyrin in complex with the C-terminal domain of S6 ATPase. Almost all of the seven ankyrin repeats of gankyrin interact, through its concave region, with the C-terminal domain of S6 ATPase. The intermolecular interactions occur through the complementary charged residues between gankyrin and S6 ATPase. Biochemical studies based on the structure of the complex revealed that gankyrin interacts with pRb in both the presence and absence of S6 ATPase; however, the E182 residue in gankyrin is essential for the pRb interaction. These results provide a structural basis for the involvement of gankyrin in the pRb degradation pathway, through its association with S6 ATPase of the 26S proteasome.

Selected figure(s)

Figure 2.
Figure 2. Structure of the Gankyrin/S6-C Complex
(A) Ribbon representation of the mouse gankyrin/S6-C complex. Each ankyrin repeat of the gankyrin is indicated by ANK1–ANK7 (blue to red). The S6-C tertiary structure is colored orange. The N and C termini of both molecules are indicated. Structural figures were generated with PyMOL (http://pymol.sourceforge.net/).
(B) van der Waals surface representation of the protein complex. Gankyrin and S6-C are shown in pink and orange, respectively.

Figure 6.
Figure 6. Model of Gankyrin in Complex with the Complete ATPase Domain of S6 ATPase
The structure of the gankyrin/S6-C complex is superposed between the S6-C domain and the C-terminal domain of the FtsH_E.coli structure for the Cα-atoms. The coloring code for the gankyrin/S6-C complex is the same as in Figure 2A, and the FtsH_E. coli structure is shown in yellow.

The above figures are reprinted by permission from Cell Press: Structure (2007, 15, 179-189) copyright 2007.

Figures were selected by an automated process.