PDBsum entry 2rpq

Transcription

PDB id: 2rpq

Contents

Protein chains

93 a.a. *

11 a.a. *

* Residue conservation analysis

PDB id:

2rpq

Name:

Transcription

Title:

Solution structure of a sumo-interacting motif of mbd1-containing chromatin-associated factor 1 bound to sumo-3

Structure:

Small ubiquitin-related modifier 2. Chain: a. Synonym: sumo-2, ubiquitin-like protein smt3b, smt3 homolog 2, sentrin-2, hsmt3, sumo-3. Engineered: yes. Activating transcription factor 7-interacting protein 1. Chain: b. Fragment: unp residues 938-981. Synonym: atfa-associated modulator, ham, atf-interacting protein,

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: this entity is chemically synthesized.

NMR struc:

20 models

Authors:

N.Sekiyama,T.Ikegami,T.Yamane,M.Ikeguchi,Y.Uchimura,D.Baba, M.Ariyoshi,H.Tochio,H.Saitoh,M.Shirakawa

Key ref:

N.Sekiyama et al. (2008). Structure of the small ubiquitin-like modifier (SUMO)-interacting motif of MBD1-containing chromatin-associated factor 1 bound to SUMO-3. J Biol Chem, 283, 35966-35975. PubMed id: 18842587

Date:

07-Jul-08 Release date: 07-Oct-08

Protein chain

P61956  (SUMO2_HUMAN) -  Small ubiquitin-related modifier 2 from Homo sapiens

Seq: 95 a.a.

Struc: 93 a.a.

Protein chain

Q6VMQ6  (MCAF1_HUMAN) -  Activating transcription factor 7-interacting protein 1 from Homo sapiens

Seq: 1270 a.a.

Struc: 11 a.a.

Enzyme reactions

• Enzyme class: Chains A, B: E.C.?

J Biol Chem 283:35966-35975 (2008)

PubMed id: 18842587

Structure of the small ubiquitin-like modifier (SUMO)-interacting motif of MBD1-containing chromatin-associated factor 1 bound to SUMO-3.

N.Sekiyama, T.Ikegami, T.Yamane, M.Ikeguchi, Y.Uchimura, D.Baba, M.Ariyoshi, H.Tochio, H.Saitoh, M.Shirakawa.

ABSTRACT

Post-translational modification by small ubiquitin-like modifier (SUMO) proteins has been implicated in the regulation of a variety of cellular events. The functions of sumoylation are often mediated by downstream effector proteins harboring SUMO-interacting motifs (SIMs) that are composed of a hydrophobic core and a stretch of acidic residues. MBD1-containing chromatin-associated factor 1 (MCAF1), a transcription repressor, interacts with SUMO-2/3 and SUMO-1, with a preference for SUMO-2/3. We used NMR spectroscopy to solve the solution structure of the SIM of MCAF1 bound to SUMO-3. The hydrophobic core of the SIM forms a parallel beta-sheet pairing with strand beta2 of SUMO-3, whereas its C-terminal acidic stretch seems to mediate electrostatic interactions with a surface area formed by basic residues of SUMO-3. The significance of these electrostatic interactions was shown by mutations of both SUMO-3 and MCAF1. The present structural and biochemical data suggest that the acidic stretch of the SIM of MCAF1 plays an important role in the binding to SUMO-3.