PDBsum entry 3zdm

Chaperone/signaling protein

PDB id: 3zdm

Contents

Protein chains

69 a.a.

50 a.a.

79 a.a.

Waters ×456

PDB id:

3zdm

Name:

Chaperone/signaling protein

Title:

Crystal structure of the sgt2 n domain and the get5 ubl domain complex

Structure:

Small glutamine-rich tetratricopeptide repeat- containing protein 2. Chain: a, b, d, e. Fragment: n-terminal domain, residues 1-72. Synonym: sgt/ubp, viral protein u-binding protein. Engineered: yes. Ubiquitin-like protein mdy2. Chain: c, f. Fragment: ubiquitin-like domain, residues 71-151.

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 511693.

Resolution:

1.80Å R-factor: 0.189 R-free: 0.226

Authors:

J.-Y.Tung,Y.-C.Li,C.-D.Hsiao

Key ref:

J.Y.Tung et al. (2013). Structure of the Sgt2 dimerization domain complexed with the Get5 UBL domain involved in the targeting of tail-anchored membrane proteins to the endoplasmic reticulum. Acta Crystallogr D Biol Crystallogr, 69, 2081-2090. PubMed id: 24100326 DOI: 10.1107/S0907444913019379

Date:

29-Nov-12 Release date: 02-Oct-13

Protein chains

Q12118  (SGT2_YEAST) -  Small glutamine-rich tetratricopeptide repeat-containing protein 2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 346 a.a.

Struc: 69 a.a.

Protein chains

Q12118  (SGT2_YEAST) -  Small glutamine-rich tetratricopeptide repeat-containing protein 2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 346 a.a.

Struc: 50 a.a.

Protein chains

Q12285  (MDY2_YEAST) -  Ubiquitin-like protein MDY2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 212 a.a.

Struc: 79 a.a.

DOI no: 10.1107/S0907444913019379

Acta Crystallogr D Biol Crystallogr 69:2081-2090 (2013)

PubMed id: 24100326

Structure of the Sgt2 dimerization domain complexed with the Get5 UBL domain involved in the targeting of tail-anchored membrane proteins to the endoplasmic reticulum.

J.Y.Tung, Y.C.Li, T.W.Lin, C.D.Hsiao.

ABSTRACT

The insertion of tail-anchored membrane (TA) proteins into the appropriate membrane is a post-translational event that requires stabilization of the transmembrane domain and targeting to the proper destination. Sgt2, a small glutamine-rich tetratricopeptide-repeat protein, is a heat-shock protein cognate (HSC) co-chaperone that preferentially binds endoplasmic reticulum-destined TA proteins and directs them to the GET pathway via Get4 and Get5. The N-terminal domain of Sgt2 seems to exert dual functions. It mediates Get5 interaction and allows substrate delivery to Get3. Following the N-terminus of Get5 is a ubiquitin-like (Ubl) domain that interacts with the N-terminus of Sgt2. Here, the crystal structure of the Sgt2 dimerization domain complexed with the Get5 Ubl domain (Sgt2N-Get5Ubl) is reported. This complex reveals an intimate interaction between one Sgt2 dimer and one Get5 monomer. This research further demonstrates that hydrophobic residues from both Sgt2 and Get5 play an important role in cell survival under heat stress. This study provides detailed molecular insights into the specific binding of this GET-pathway complex.