PDBsum entry 2asq

Protein binding

PDB id: 2asq

Contents

Protein chains

77 a.a. *

14 a.a. *

* Residue conservation analysis

PDB id:

2asq

Name:

Protein binding

Title:

Solution structure of sumo-1 in complex with a sumo-binding motif (sbm)

Structure:

Small ubiquitin-related modifier 1. Chain: a. Fragment: structured region of sumo-1 (residues 21-97). Synonym: sumo-1, ubiquitin-like protein smt3c, smt3 homolog 3, ubiquitin-homology domain protein pic1, ubiquitin-like protein ubl1, gap modifying protein 1, gmp1, sentrin. Engineered: yes. Protein inhibitor of activated stat2. Chain: b.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: sumo1, smt3c, smt3h3, ubl1. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: pias2, piasx.

NMR struc:

10 models

Authors:

J.Song,Z.Zhang,W.Hu,Y.Chen

Key ref:

J.Song et al. (2005). Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation. J Biol Chem, 280, 40122-40129. PubMed id: 16204249 DOI: 10.1074/jbc.M507059200

Date:

23-Aug-05 Release date: 11-Oct-05

Protein chain

P63165  (SUMO1_HUMAN) -  Small ubiquitin-related modifier 1 from Homo sapiens

Seq: 101 a.a.

Struc: 77 a.a.

Protein chain

O75928  (PIAS2_HUMAN) -  E3 SUMO-protein ligase PIAS2 from Homo sapiens

Seq: 621 a.a.

Struc: 14 a.a.

Enzyme reactions

• Enzyme class 2: Chain A: E.C.?
• Enzyme class 3: Chain B: E.C.2.3.2.- - ?????

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

DOI no: 10.1074/jbc.M507059200

J Biol Chem 280:40122-40129 (2005)

PubMed id: 16204249

Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation.

J.Song, Z.Zhang, W.Hu, Y.Chen.

ABSTRACT

Sumoylation has recently been identified as an important mechanism that regulates protein interactions and localization in essential cellular functions, such as gene transcription, subnuclear structure formation, viral infection, and cell cycle progression. A SUMO binding amino acid sequence motif (SBM), which recognizes the SUMO moiety of modified proteins in sumoylation-dependent cellular functions, has been consistently identified by several recent studies. To understand the mechanism of SUMO recognition by the SBM, we have solved the solution structure of SUMO-1 in complex with a peptide containing the SBM derived from the protein PIASX (KVDVIDLTIESSSDEEEDPPAKR). Surprisingly, the structure reveals that the bound orientation of the SBM can reverse depending on the sequence context. The structure also reveals a novel mechanism of recognizing target sequences by a ubiquitin-like module. Unlike ubiquitin binding motifs, which all form helices and bind to the main beta-sheet of ubiquitin, the SBM forms an extended structure that binds between the alpha-helix and a beta-strand of SUMO-1. This study provides a clear mechanism of the SBM sequence variations and its recognition of the SUMO moiety in sumoylated proteins.

Selected figure(s)

Figure 2.
FIGURE 2. Solution structure of the PIASX-P·SUMO-1 complex. A, stereo view of the superimposed C[ ]traces of 10 NMR structures of the PIASX-P·SUMO-1 complex. SUMO-1 is shown in deep pink, and residues 2-8 and other residues of the PIASX-P peptide are shown in blue and orange, respectively. B, stereo view of a ribbon diagram of a representative structure from the ensemble of NMR structures in the same orientation. The color code is the same as in A.

Figure 3.
FIGURE 3. The binding interface of the PIASX-P·SUMO-1 complex. A, stereo view of a ribbon diagram of SUMO-1 (pink) in complex with the PIASX-P peptide (light blue). The side chains of the key interface residues (from which the intermolecular NOEs were observed) from SUMO-1 are shown in deep pink, and the side chains of residues of PIASX-P involved in the interaction are shown in blue. B, a similar view as that shown in A except that SUMO-1 is shown as a surface representation with hydrophobic and aromatic residues indicated in green. C, a similar view as in B with the surface of SUMO-1 color-coded according to the electrostatic potentials. Red to blue corresponds to negative to positive electrostatic potentials. The side chains of residues 1-8 of the peptide are shown with acidic side chains indicated in red, and basic side chains indicated in blue. The side chains of all others residues are indicated in green.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2005, 280, 40122-40129) copyright 2005.

Figures were selected by an automated process.