PDBsum entry 4mbe

Protein transport, transcription

PDB id: 4mbe

Contents

Protein chains

149 a.a.

50 a.a.

94 a.a.

51 a.a.

88 a.a.

Ligands

VAL-LEU-PRO-THR-VAL-GLY-PHE-ASP-PHE-ILE

LEU-PRO-THR-VAL-GLY-PHE-ASP-PHE-ILE

ASP-LYS-GLU-SER-ILE-VAL

GLU-SER-ILE-VAL

Metals

_CA ×4

Waters ×33

PDB id:

4mbe

Name:

Protein transport, transcription

Title:

Sac3:sus1:cdc31:nup1 complex

Structure:

Cell division control protein 31. Chain: a, d. Synonym: nuclear pore protein cdc31, nucleoporin cdc31. Engineered: yes. Nuclear mRNA export protein sac3. Chain: b, e. Fragment: cdc31 interacting region, residues 753-805. Synonym: leucine permease transcriptional regulator. Engineered: yes.

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: cdc31, dsk1, yor257w. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: sac3, lep1, ydr159w, yd8358.13. Gene: sus1, ybr111w-a.

Resolution:

2.61Å R-factor: 0.202 R-free: 0.236

Authors:

D.Jani,B.Meineke,M.Stewart

Key ref:

D.Jani et al. (2014). Structural basis for binding the TREX2 complex to nuclear pores, GAL1 localisation and mRNA export. Nucleic Acids Res, 42, 6686-6697. PubMed id: 24705649 DOI: 10.1093/nar/gku252

Date:

19-Aug-13 Release date: 02-Jul-14

Protein chains

P06704  (CDC31_YEAST) -  Cell division control protein 31 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 161 a.a.

Struc: 149 a.a.

Protein chain

P46674  (SAC3_YEAST) -  Nuclear mRNA export protein SAC3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 1301 a.a.

Struc: 50 a.a.

Protein chain

Q6WNK7  (SUS1_YEAST) -  Transcription and mRNA export factor SUS1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 96 a.a.

Struc: 94 a.a.

Protein chain

P46674  (SAC3_YEAST) -  Nuclear mRNA export protein SAC3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 1301 a.a.

Struc: 51 a.a.

Protein chain

Q6WNK7  (SUS1_YEAST) -  Transcription and mRNA export factor SUS1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 96 a.a.

Struc: 88 a.a.

DOI no: 10.1093/nar/gku252

Nucleic Acids Res 42:6686-6697 (2014)

PubMed id: 24705649

Structural basis for binding the TREX2 complex to nuclear pores, GAL1 localisation and mRNA export.

D.Jani, E.Valkov, M.Stewart.

ABSTRACT

The conserved Sac3:Thp1:Sem1:Sus1:Cdc31 (TREX2) complex binds to nuclear pore complexes (NPCs) and, in addition to integrating mRNA nuclear export with preceding steps in the gene expression pathway, facilitates re-positioning of highly regulated actively transcribing genes (such as GAL1) to NPCs. Although TREX2 is thought to bind NPC protein Nup1, defining the precise role of this interaction has been frustrated by the complex pleiotropic phenotype exhibited by nup1Δ strains. To provide a structural framework for understanding the binding of TREX2 to NPCs and its function in the gene expression pathway, we have determined the structure of the Nup1:TREX2 interaction interface and used this information to engineer a Sac3 variant that impairs NPC binding while not compromising TREX2 assembly. This variant inhibited the NPC association of both de-repressed and activated GAL1 and also produced mRNA export and growth defects. These results indicate that the TREX2:Nup1 interaction facilitates the efficient nuclear export of bulk mRNA together with the re-positioning of GAL1 to NPCs that is required for transcriptional control that is mediated by removal of SUMO from repressors by NPC-bound Ulp1.