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4mbe

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Sac3:Sus1:Cdc31:Nup1 complex

Structural highlights

4mbe is a 10 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.612Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CDC31_YEAST Functions as a component of the nuclear pore complex (NPC) and the spindle pole body (SPB) half-bridge. At the SPB, it is recruited by KAR1 and MPS3 to the SPB half-bridge and involved in the initial steps of SPB duplication. It probably plays a similar role in de novo assembly of NPCs at the nuclear envelope. Also involved in connection with the protein kinase KIC1 in the maintenance of cell morphology and integrity.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Publication Abstract from PubMed

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 nup1Delta 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.

Structural basis for binding the TREX2 complex to nuclear pores, GAL1 localisation and mRNA export.,Jani D, Valkov E, Stewart M Nucleic Acids Res. 2014 Apr 4. PMID:24705649^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Biggins S, Rose MD. Direct interaction between yeast spindle pole body components: Kar1p is required for Cdc31p localization to the spindle pole body. J Cell Biol. 1994 May;125(4):843-52. PMID:8188750
↑ Vallen EA, Ho W, Winey M, Rose MD. Genetic interactions between CDC31 and KAR1, two genes required for duplication of the microtubule organizing center in Saccharomyces cerevisiae. Genetics. 1994 Jun;137(2):407-22. PMID:8070654
↑ Sullivan DS, Biggins S, Rose MD. The yeast centrin, cdc31p, and the interacting protein kinase, Kic1p, are required for cell integrity. J Cell Biol. 1998 Nov 2;143(3):751-65. PMID:9813095
↑ Ivanovska I, Rose MD. Fine structure analysis of the yeast centrin, Cdc31p, identifies residues specific for cell morphology and spindle pole body duplication. Genetics. 2001 Feb;157(2):503-18. PMID:11156974
↑ Jaspersen SL, Giddings TH Jr, Winey M. Mps3p is a novel component of the yeast spindle pole body that interacts with the yeast centrin homologue Cdc31p. J Cell Biol. 2002 Dec 23;159(6):945-56. Epub 2002 Dec 16. PMID:12486115 doi:http://dx.doi.org/10.1083/jcb.200208169
↑ Kilmartin JV. Sfi1p has conserved centrin-binding sites and an essential function in budding yeast spindle pole body duplication. J Cell Biol. 2003 Sep 29;162(7):1211-21. Epub 2003 Sep 22. PMID:14504268 doi:http://dx.doi.org/10.1083/jcb.200307064
↑ Jani D, Valkov E, Stewart M. Structural basis for binding the TREX2 complex to nuclear pores, GAL1 localisation and mRNA export. Nucleic Acids Res. 2014 Apr 4. PMID:24705649 doi:http://dx.doi.org/10.1093/nar/gku252

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4mbe"

Categories: Large Structures | Saccharomyces cerevisiae S288C | Jani D | Meineke B | Stewart M

@@ Line 1: / Line 1: @@
 ==Sac3:Sus1:Cdc31:Nup1 complex==
-<StructureSection load='4mbe' size='340' side='right' caption='[[4mbe]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
+<StructureSection load='4mbe' size='340' side='right'caption='[[4mbe]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4mbe]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MBE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MBE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4mbe]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MBE FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.612&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mbe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mbe RCSB], [http://www.ebi.ac.uk/pdbsum/4mbe PDBsum]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-<table>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4mbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mbe OCA], [https://pdbe.org/4mbe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mbe RCSB], [https://www.ebi.ac.uk/pdbsum/4mbe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mbe ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CDC31_YEAST CDC31_YEAST] Functions as a component of the nuclear pore complex (NPC) and the spindle pole body (SPB) half-bridge. At the SPB, it is recruited by KAR1 and MPS3 to the SPB half-bridge and involved in the initial steps of SPB duplication. It probably plays a similar role in de novo assembly of NPCs at the nuclear envelope. Also involved in connection with the protein kinase KIC1 in the maintenance of cell morphology and integrity.<ref>PMID:8188750</ref> <ref>PMID:8070654</ref> <ref>PMID:9813095</ref> <ref>PMID:11156974</ref> <ref>PMID:12486115</ref> <ref>PMID:14504268</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 14: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4mbe" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Jani, D.]]
+[[Category: Large Structures]]
-[[Category: Meineke, B.]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Stewart, M.]]
+[[Category: Jani D]]
-[[Category: Mrna]]
+[[Category: Meineke B]]
-[[Category: Mrna nuclear export]]
+[[Category: Stewart M]]
-[[Category: Protein transport]]
-[[Category: Transcription]]

4mbe

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Current revision

Sac3:Sus1:Cdc31:Nup1 complex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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