PDBsum entry 1v66

Ligase

PDB id: 1v66

Contents

Protein chain

65 a.a. *

* Residue conservation analysis

PDB id:

1v66

Name:

Ligase

Title:

Solution structure of human p53 binding domain of pias-1

Structure:

Protein inhibitor of activated stat protein 1. Chain: a. Fragment: residues 1-65. Synonym: protein inhibitor of activated stat-1, pias-1, gu binding protein, gbp, RNA helicase ii binding protein, dead/h box-binding protein 1. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

S.Okubo,F.Hara,Y.Tsuchida,S.Shimotakahara,S.Suzuki,H.Hatanaka, S.Yokoyama,H.Tanaka,H.Yasuda,H.Shindo,Riken Structural Genomics/proteomics Initiative (Rsgi)

Key ref:

S.Okubo et al. (2004). NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomers. J Biol Chem, 279, 31455-31461. PubMed id: 15133049 DOI: 10.1074/jbc.M403561200

Date:

27-Nov-03 Release date: 07-Dec-04

Protein chain

O75925  (PIAS1_HUMAN) -  E3 SUMO-protein ligase PIAS1 from Homo sapiens

Seq: 651 a.a.

Struc: 65 a.a.

Enzyme reactions

• Enzyme class: E.C.2.3.2.- - ?????

DOI no: 10.1074/jbc.M403561200

J Biol Chem 279:31455-31461 (2004)

PubMed id: 15133049

NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomers.

S.Okubo, F.Hara, Y.Tsuchida, S.Shimotakahara, S.Suzuki, H.Hatanaka, S.Yokoyama, H.Tanaka, H.Yasuda, H.Shindo.

ABSTRACT

A member of the PIAS (protein inhibitor of activated STAT) family of proteins, PIAS1, have been reported to serve as an E3-type SUMO ligase for tumor suppressor p53 and its own. It also was proposed that the N-terminal domain of PIAS1 interacts with DNA as well as p53. Extensive biochemical studies have been devoted recently to understand sumoylations and its biological implications, whereas the structural aspects of the PIAS family and the mechanism of its interactions with various factors are less well known to date. In this study, the three-dimensional structure of the N-terminal domain (residues 1-65) of SUMO ligase PIAS1 was determined by NMR spectroscopy. The structure revealed a unique four-helix bundle with a topology of an up-down-extended loop-down-up, a part of which the helix-extended loop-helix represented the SAP (SAF-A/B, Acinus, and PIAS) motif. Thus, this N-terminal domain may be referred to as a four-helix SAP domain. The glutathione S-transferase pull-down assay demonstrated that this domain possesses a binding ability to tumor suppressor p53, a target protein for sumoylation by PIAS1, whereas gel mobility assays showed that it has a strong affinity toward A/T-rich DNA. An NMR analysis of the four-helix SAP domain complexed with the 16-bp-long DNA demonstrated that one end of the four-helix bundle is the binding site and may fit into the minor groove of DNA. The three-dimensional structure and its binding duality are discussed in conjunction with the biological functions of PIAS1 as a SUMO ligase.

Selected figure(s)

Figure 6.
FIG. 6. The highly perturbed residues of PIA-(1-65) upon its binding to DNA16 are colored in red ( > 0.3 ppm) and pink (0.3 ppm > > 0.1 ppm) in the side view (a) and the top view (b). Side chains of basic residues also are depicted in the model. C, C terminus; N, N terminus.

Figure 7.
FIG. 7. Stereoviews of the superimposed ribbon diagrams for the four-helix SAP domain, PIA-(1-65), with protease inhibitor Iceberg (Protein Data Bank code 1DGN [PDB] ) (a), the C-terminal domain of bacteriophage T4 endonuclease VII (Protein Data Bank code 1EN7 [PDB] ) (b), and the C-terminal domain of Ku70 (Protein Data Bank code 1JJR [PDB] ) (c). The N-terminal domain of PIAS1 is in blue, and the other domains are in red.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2004, 279, 31455-31461) copyright 2004.

Figures were selected by an automated process.