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==Crystal Structure of the yeast Sec23/24 heterodimer==
==Crystal Structure of the yeast Sec23/24 heterodimer==
<StructureSection load='1m2v' size='340' side='right' caption='[[1m2v]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
<StructureSection load='1m2v' size='340' side='right'caption='[[1m2v]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1m2v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M2V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M2V FirstGlance]. <br>
<table><tr><td colspan='2'>[[1m2v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M2V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M2V FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.75&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1m2o|1m2o]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Sec23 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), Sar1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m2v OCA], [https://pdbe.org/1m2v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m2v RCSB], [https://www.ebi.ac.uk/pdbsum/1m2v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m2v ProSAT]</span></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=1m2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m2v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1m2v RCSB], [http://www.ebi.ac.uk/pdbsum/1m2v PDBsum]</span></td></tr>
</table>
<table>
== Function ==
[https://www.uniprot.org/uniprot/SEC23_YEAST SEC23_YEAST] Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SEC23 interacts with BET3 in order to target TRAPPI complex to COPII involved in internalisation of plasma membrane proteins like the maltose transporter.<ref>PMID:2670558</ref> <ref>PMID:6996832</ref> <ref>PMID:7026045</ref> <ref>PMID:3293799</ref> <ref>PMID:3049622</ref> <ref>PMID:2188733</ref> <ref>PMID:1498369</ref> <ref>PMID:7925484</ref> <ref>PMID:8451644</ref> <ref>PMID:8548805</ref> <ref>PMID:8909535</ref> <ref>PMID:9427388</ref> <ref>PMID:9023343</ref> <ref>PMID:9624457</ref> <ref>PMID:9428766</ref> <ref>PMID:10198022</ref> <ref>PMID:11086000</ref> <ref>PMID:10720463</ref> <ref>PMID:12941276</ref> <ref>PMID:14627716</ref> <ref>PMID:16269340</ref> <ref>PMID:17287728</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m2/1m2v_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m2/1m2v_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m2v ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
COPII-coated vesicles form on the endoplasmic reticulum by the stepwise recruitment of three cytosolic components: Sar1-GTP to initiate coat formation, Sec23/24 heterodimer to select SNARE and cargo molecules, and Sec13/31 to induce coat polymerization and membrane deformation. Crystallographic analysis of the Saccharomyces cerevisiae Sec23/24-Sar1 complex reveals a bow-tie-shaped structure, 15 nm long, with a membrane-proximal surface that is concave and positively charged to conform to the size and acidic-phospholipid composition of the COPII vesicle. Sec23 and Sar1 form a continuous surface stabilized by a non-hydrolysable GTP analogue, and Sar1 has rearranged from the GDP conformation to expose amino-terminal residues that will probably embed in the bilayer. The GTPase-activating protein (GAP) activity of Sec23 involves an arginine side chain inserted into the Sar1 active site. These observations establish the structural basis for GTP-dependent recruitment of a vesicular coat complex, and for uncoating through coat-controlled GTP hydrolysis.
Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat.,Bi X, Corpina RA, Goldberg J Nature. 2002 Sep 19;419(6904):271-7. PMID:12239560<ref>PMID:12239560</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Bi, X.]]
[[Category: Bi X]]
[[Category: Corpina, R A.]]
[[Category: Corpina RA]]
[[Category: Goldberg, J.]]
[[Category: Goldberg J]]
[[Category: Beta barrel]]
[[Category: Gelsolin domain]]
[[Category: Protein transport]]
[[Category: Vwa domain]]
[[Category: Zinc-finger]]

Latest revision as of 10:39, 14 February 2024

Crystal Structure of the yeast Sec23/24 heterodimerCrystal Structure of the yeast Sec23/24 heterodimer

Structural highlights

1m2v is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.75Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SEC23_YEAST Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SEC23 interacts with BET3 in order to target TRAPPI complex to COPII involved in internalisation of plasma membrane proteins like the maltose transporter.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] [13] [14] [15] [16] [17] [18] [19] [20] [21] [22]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Hicke L, Schekman R. Yeast Sec23p acts in the cytoplasm to promote protein transport from the endoplasmic reticulum to the Golgi complex in vivo and in vitro. EMBO J. 1989 Jun;8(6):1677-84. PMID:2670558
  2. ↑ Novick P, Field C, Schekman R. Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell. 1980 Aug;21(1):205-15. PMID:6996832
  3. ↑ Novick P, Ferro S, Schekman R. Order of events in the yeast secretory pathway. Cell. 1981 Aug;25(2):461-9. PMID:7026045
  4. ↑ Baker D, Hicke L, Rexach M, Schleyer M, Schekman R. Reconstitution of SEC gene product-dependent intercompartmental protein transport. Cell. 1988 Jul 29;54(3):335-44. PMID:3293799
  5. ↑ Ruohola H, Kabcenell AK, Ferro-Novick S. Reconstitution of protein transport from the endoplasmic reticulum to the Golgi complex in yeast: the acceptor Golgi compartment is defective in the sec23 mutant. J Cell Biol. 1988 Oct;107(4):1465-76. PMID:3049622
  6. ↑ Kaiser CA, Schekman R. Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway. Cell. 1990 May 18;61(4):723-33. PMID:2188733
  7. ↑ Hicke L, Yoshihisa T, Schekman R. Sec23p and a novel 105-kDa protein function as a multimeric complex to promote vesicle budding and protein transport from the endoplasmic reticulum. Mol Biol Cell. 1992 Jun;3(6):667-76. PMID:1498369
  8. ↑ Liang S, Lacroute F, Kepes F. Multicopy STS1 restores both protein transport and ribosomal RNA stability in a new yeast sec23 mutant allele. Eur J Cell Biol. 1993 Dec;62(2):270-81. PMID:7925484
  9. ↑ Yoshihisa T, Barlowe C, Schekman R. Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum. Science. 1993 Mar 5;259(5100):1466-8. PMID:8451644
  10. ↑ Bednarek SY, Ravazzola M, Hosobuchi M, Amherdt M, Perrelet A, Schekman R, Orci L. COPI- and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast. Cell. 1995 Dec 29;83(7):1183-96. PMID:8548805
  11. ↑ Kuehn MJ, Schekman R, Ljungdahl PO. Amino acid permeases require COPII components and the ER resident membrane protein Shr3p for packaging into transport vesicles in vitro. J Cell Biol. 1996 Nov;135(3):585-95. PMID:8909535
  12. ↑ Sutterlin C, Doering TL, Schimmoller F, Schroder S, Riezman H. Specific requirements for the ER to Golgi transport of GPI-anchored proteins in yeast. J Cell Sci. 1997 Nov;110 ( Pt 21):2703-14. PMID:9427388
  13. ↑ Campbell JL, Schekman R. Selective packaging of cargo molecules into endoplasmic reticulum-derived COPII vesicles. Proc Natl Acad Sci U S A. 1997 Feb 4;94(3):837-42. PMID:9023343
  14. ↑ Morin-Ganet MN, Rambourg A, Clermont Y, Kepes F. Role of endoplasmic reticulum-derived vesicles in the formation of Golgi elements in sec23 and sec18 Saccharomyces Cerevisiae mutants. Anat Rec. 1998 Jun;251(2):256-64. PMID:9624457
  15. ↑ Kuehn MJ, Herrmann JM, Schekman R. COPII-cargo interactions direct protein sorting into ER-derived transport vesicles. Nature. 1998 Jan 8;391(6663):187-90. PMID:9428766 doi:http://dx.doi.org/10.1038/34438
  16. ↑ Penalver E, Lucero P, Moreno E, Lagunas R. Clathrin and two components of the COPII complex, Sec23p and Sec24p, could be involved in endocytosis of the Saccharomyces cerevisiae maltose transporter. J Bacteriol. 1999 Apr;181(8):2555-63. PMID:10198022
  17. ↑ Shimoni Y, Kurihara T, Ravazzola M, Amherdt M, Orci L, Schekman R. Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae. J Cell Biol. 2000 Nov 27;151(5):973-84. PMID:11086000
  18. ↑ Matsuoka K, Schekman R. The use of liposomes to study COPII- and COPI-coated vesicle formation and membrane protein sorting. Methods. 2000 Apr;20(4):417-28. PMID:10720463 doi:10.1006/meth.2000.0955
  19. ↑ Mossessova E, Bickford LC, Goldberg J. SNARE selectivity of the COPII coat. Cell. 2003 Aug 22;114(4):483-95. PMID:12941276
  20. ↑ Sato K, Nakano A. Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting. J Biol Chem. 2004 Jan 9;279(2):1330-5. Epub 2003 Nov 19. PMID:14627716 doi:10.1074/jbc.C300457200
  21. ↑ Schuldiner M, Collins SR, Thompson NJ, Denic V, Bhamidipati A, Punna T, Ihmels J, Andrews B, Boone C, Greenblatt JF, Weissman JS, Krogan NJ. Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile. Cell. 2005 Nov 4;123(3):507-19. PMID:16269340 doi:S0092-8674(05)00868-8
  22. ↑ Cai H, Yu S, Menon S, Cai Y, Lazarova D, Fu C, Reinisch K, Hay JC, Ferro-Novick S. TRAPPI tethers COPII vesicles by binding the coat subunit Sec23. Nature. 2007 Feb 22;445(7130):941-4. Epub 2007 Feb 7. PMID:17287728 doi:http://dx.doi.org/10.1038/nature05527

1m2v, resolution 2.75Å

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