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PDBsum entry 3fwc
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protein ligands Protein-protein interface(s) links
Cell cycle, transcription PDB id
3fwc

 

 

 

 

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Contents
Protein chains
145 a.a. *
83 a.a. *
87 a.a. *
92 a.a. *
78 a.a. *
Ligands
SO4 ×4
Waters ×122
* Residue conservation analysis
PDB id:
3fwc
Name: Cell cycle, transcription
Title: Sac3:sus1:cdc31 complex
Structure: Cell division control protein 31. Chain: a, e, i, m. Synonym: nucleoporin cdc31, nuclear pore protein cdc31. Engineered: yes. Nuclear mRNA export protein sac3. Chain: b, f, j, n. Fragment: residues 723-805. Synonym: leucine permease transcriptional regulator. Engineered: yes.
Source: Saccharomyces cerevisiae. Brewer's yeast,lager beer yeast,yeast. Organism_taxid: 4932. Gene: cdc31, dsk1, yor257w. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: lep1, sac3, yd8358.13, ydr159w. Gene: sus1, ybr111w-a.
Resolution:
2.70Å     R-factor:   0.214     R-free:   0.265
Authors: M.Stewart,D.Jani
Key ref:
D.Jani et al. (2009). Sus1, Cdc31, and the Sac3 CID region form a conserved interaction platform that promotes nuclear pore association and mRNA export. Mol Cell, 33, 727-737. PubMed id: 19328066 DOI: 10.1016/j.molcel.2009.01.033
Date:
17-Jan-09     Release date:   14-Apr-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P06704  (CDC31_YEAST) -  Cell division control protein 31 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		161 a.a.
145 a.a.
Protein chains
Pfam   ArchSchema ?
P46674  (SAC3_YEAST) -  Nuclear mRNA export protein SAC3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		1301 a.a.
83 a.a.*
Protein chains
Pfam   ArchSchema ?
Q6WNK7  (SUS1_YEAST) -  Transcription and mRNA export factor SUS1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		96 a.a.
87 a.a.
Protein chains
Pfam   ArchSchema ?
Q6WNK7  (SUS1_YEAST) -  Transcription and mRNA export factor SUS1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		96 a.a.
92 a.a.
Protein chain
Pfam   ArchSchema ?
P46674  (SAC3_YEAST) -  Nuclear mRNA export protein SAC3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		1301 a.a.
78 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
DOI no: 10.1016/j.molcel.2009.01.033 Mol Cell 33:727-737 (2009)
PubMed id: 19328066  
 
 
Sus1, Cdc31, and the Sac3 CID region form a conserved interaction platform that promotes nuclear pore association and mRNA export.
D.Jani, S.Lutz, N.J.Marshall, T.Fischer, A.Köhler, A.M.Ellisdon, E.Hurt, M.Stewart.
 
  ABSTRACT  
 
The yeast Sac3:Cdc31:Sus1:Thp1 (TREX-2) complex facilitates the repositioning and association of actively transcribing genes with nuclear pores (NPCs)-"gene gating"-that is central to integrating transcription, processing, and mRNA nuclear export. We present here the crystal structure of Sus1 and Cdc31 bound to a central region of Sac3 (the CID domain) that is crucial for its function. Sac3(CID) forms a long, gently undulating alpha helix around which one Cdc31 and two Sus1 chains are wrapped. Sus1 has an articulated helical hairpin fold that facilitates its wrapping around Sac3. In vivo studies using engineered mutations that selectively disrupted binding of individual chains to Sac3 indicated that Sus1 and Cdc31 function synergistically to promote NPC association of TREX-2 and mRNA nuclear export. These data indicate Sac3(CID) provides a scaffold within TREX-2 to integrate interactions between protein complexes to facilitate the coupling of transcription and mRNA export during gene expression.
 
  Selected figure(s)  
 
Figure 2.
Overview of Crystal Structure of the Sac3^CID:Cdc31:Sus1 Complex (A) Surface view. (B) Secondary structure schematic. Cdc31 is yellow, Sac3 is red, Sus1A is blue, and Sus1B is cyan. Residues 723 --805 of Sac3 form a continuous, 12.5 nm-long, gently undulating, [alpha] helix to which one Cdc31 and two Sus1 (Sus1A and Sus1B) chains bind. (C) Schematic of the principal residues that are buried in the interfaces between Sac3 and its partners. Dashed lines represent putative H bonds. Mol Cell. 2009 March 27; 33(6-2): 727–737. doi: 10.1016/j.molcel.2009.01.033. Copyright [copyright] 2009 ELL & Excerpta Medica
Figure 3.
Sus1:Sac3 Interaction (A and B) The hinges between the rigid Sus1 [alpha] helices enable the molecule to wrap around the Sac3^CID helix, shown in red. (C) End-on view showing Sus1 wrapping around the Sac3 helix like fingers gripping a rod. (D) Sus1 sequences showing the conservation of both the helices ([alpha]1, [alpha]2, [alpha]3, [alpha]4, and [alpha]5) and the hinges between them. Single Gly residues (yellow) form the hinges between helices [alpha]1/[alpha]2 and [alpha]2/[alpha]3. A kink introduced by a Pro in helix [alpha]4 enhances the intimacy of the contact with Sac3. Mol Cell. 2009 March 27; 33(6-2): 727–737. doi: 10.1016/j.molcel.2009.01.033. Copyright [copyright] 2009 ELL & Excerpta Medica
 
  The above figures are reprinted from an Open Access publication published by Cell Press: Mol Cell (2009, 33, 727-737) copyright 2009.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
22343721 A.M.Ellisdon, L.Dimitrova, E.Hurt, and M.Stewart (2012).
Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex.
  Nat Struct Mol Biol, 19, 328-336.
PDB codes: 3t5v 3t5x
20385085 A.Köhler, and E.Hurt (2010).
Gene regulation by nucleoporins and links to cancer.
  Mol Cell, 38, 6.  
20434206 A.Köhler, E.Zimmerman, M.Schneider, E.Hurt, and N.Zheng (2010).
Structural basis for assembly and activation of the heterotetrameric SAGA histone H2B deubiquitinase module.
  Cell, 141, 606-617.
PDB code: 3m99
20007317 A.M.Ellisdon, D.Jani, A.Köhler, E.Hurt, and M.Stewart (2010).
Structural basis for the interaction between yeast Spt-Ada-Gcn5 acetyltransferase (SAGA) complex components Sgf11 and Sus1.
  J Biol Chem, 285, 3850-3856.
PDB codes: 3kik 3kjl
20230609 B.Cuenca-Bono, V.García-Molinero, P.Pascual-García, E.García-Oliver, A.Llopis, and S.Rodríguez-Navarro (2010).
A novel link between Sus1 and the cytoplasmic mRNA decay machinery suggests a broad role in mRNA metabolism.
  BMC Cell Biol, 11, 19.  
20571586 C.Strambio-De-Castillia, M.Niepel, and M.P.Rout (2010).
The nuclear pore complex: bridging nuclear transport and gene regulation.
  Nat Rev Mol Cell Biol, 11, 490-501.  
20048002 D.V.Kopytova, A.V.Orlova, A.N.Krasnov, D.Y.Gurskiy, J.V.Nikolenko, E.N.Nabirochkina, Y.V.Shidlovskii, and S.G.Georgieva (2010).
Multifunctional factor ENY2 is associated with the THO complex and promotes its recruitment onto nascent mRNA.
  Genes Dev, 24, 86-96.  
  21327099 M.B.Faza, S.Kemmler, and V.G.Panse (2010).
Sem1: A versatile "molecular glue"?
  Nucleus, 1, 12-17.  
20719516 M.Stewart (2010).
Nuclear export of mRNA.
  Trends Biochem Sci, 35, 609-617.  
20395473 N.L.Samara, A.B.Datta, C.E.Berndsen, X.Zhang, T.Yao, R.E.Cohen, and C.Wolberger (2010).
Structural insights into the assembly and function of the SAGA deubiquitinating module.
  Science, 328, 1025-1029.
PDB codes: 3mhh 3mhs
19843313 Q.Lu, X.Tang, G.Tian, F.Wang, K.Liu, V.Nguyen, S.E.Kohalmi, W.A.Keller, E.W.Tsang, J.J.Harada, S.J.Rothstein, and Y.Cui (2010).
Arabidopsis homolog of the yeast TREX-2 mRNA export complex: components and anchoring nucleoporin.
  Plant J, 61, 259-270.  
20212085 S.Kundu, and C.L.Peterson (2010).
Dominant role for signal transduction in the transcriptional memory of yeast GAL genes.
  Mol Cell Biol, 30, 2330-2340.  
  21326821 V.O.Wickramasinghe, M.Stewart, and R.A.Laskey (2010).
GANP enhances the efficiency of mRNA nuclear export in mammalian cells.
  Nucleus, 1, 393-396.  
20005110 V.O.Wickramasinghe, P.I.McMurtrie, A.D.Mills, Y.Takei, S.Penrhyn-Lowe, Y.Amagase, S.Main, J.Marr, M.Stewart, and R.A.Laskey (2010).
mRNA export from mammalian cell nuclei is dependent on GANP.
  Curr Biol, 20, 25-31.  
19854129 R.Perales, and D.Bentley (2009).
"Cotranscriptionality": the transcription elongation complex as a nexus for nuclear transactions.
  Mol Cell, 36, 178-191.  
19552647 S.M.Kelly, and A.H.Corbett (2009).
Messenger RNA export from the nucleus: a series of molecular wardrobe changes.
  Traffic, 10, 1199-1208.  
19609321 S.Rodríguez-Navarro (2009).
Insights into SAGA function during gene expression.
  EMBO Rep, 10, 843-850.  
19805193 V.Nagy, K.C.Hsia, E.W.Debler, M.Kampmann, A.M.Davenport, G.Blobel, and A.Hoelz (2009).
Structure of a trimeric nucleoporin complex reveals alternate oligomerization states.
  Proc Natl Acad Sci U S A, 106, 17693-17698.
PDB code: 3iko
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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