4bzi

From Proteopedia

(Difference between revisions)

Revision as of 17:17, 7 September 2022

The structure of the COPII coat assembled on membranes

4bzi, resolution 23.00Å

Structural highlights

4bzi is a 12 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Experimental data:	Check to display Experimental Data
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]

References

↑ 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
↑ 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
↑ Novick P, Ferro S, Schekman R. Order of events in the yeast secretory pathway. Cell. 1981 Aug;25(2):461-9. PMID:7026045
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ Mossessova E, Bickford LC, Goldberg J. SNARE selectivity of the COPII coat. Cell. 2003 Aug 22;114(4):483-95. PMID:12941276
↑ 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
↑ 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
↑ 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

1 Structural highlights
2 Function
3 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <SX load='4bzi' size='340' side='right' viewer='molstar' caption='[[4bzi]], [[Resolution|resolution]] 23.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4bzi]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BZI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4BZI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4bzi]] is a 12 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=4BZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BZI FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bzj|4bzj]], [[4bzk|4bzk]]</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=4bzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bzi OCA], [https://pdbe.org/4bzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bzi RCSB], [https://www.ebi.ac.uk/pdbsum/4bzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bzi ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=4bzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bzi OCA], [http://pdbe.org/4bzi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bzi RCSB], [http://www.ebi.ac.uk/pdbsum/4bzi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bzi ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[[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>
-Coat protein complex II (COPII) mediates formation of the membrane vesicles that export newly synthesised proteins from the endoplasmic reticulum. The inner COPII proteins bind to cargo and membrane, linking them to the outer COPII components that form a cage around the vesicle. Regulated flexibility in coat architecture is essential for transport of a variety of differently sized cargoes, but structural data on the assembled coat has not been available. We have used cryo-electron tomography and subtomogram averaging to determine the structure of the complete, membrane-assembled COPII coat. We describe a novel arrangement of the outer coat and find that the inner coat can assemble into regular lattices. The data reveal how coat subunits interact with one another and with the membrane, suggesting how coordinated assembly of inner and outer coats can mediate and regulate packaging of vesicles ranging from small spheres to large tubular carriers. DOI:http://dx.doi.org/10.7554/eLife.00951.001.
-The structure of the COPII transport-vesicle coat assembled on membranes.,Zanetti G, Prinz S, Daum S, Meister A, Schekman R, Bacia K, Briggs JA Elife. 2013 Sep 17;2:e00951. doi: 10.7554/eLife.00951. PMID:24062940<ref>PMID:24062940</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4bzi" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </SX>
-[[Category: Atcc 18824]]
 [[Category: Large Structures]]
-[[Category: Bacia, K]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Briggs, J A.G]]
+[[Category: Bacia K]]
-[[Category: Daum, S]]
+[[Category: Briggs JAG]]
-[[Category: Meister, A]]
+[[Category: Daum S]]
-[[Category: Prinz, S]]
+[[Category: Meister A]]
-[[Category: Schekman, R]]
+[[Category: Prinz S]]
-[[Category: Zanetti, G]]
+[[Category: Schekman R]]
-[[Category: Sar1]]
+[[Category: Zanetti G]]
-[[Category: Sec23]]
-[[Category: Sec24]]
-[[Category: Secretion]]
-[[Category: Trafficking]]
-[[Category: Transport protein]]

4bzi

From Proteopedia

Revision as of 17:17, 7 September 2022

The structure of the COPII coat assembled on membranes

Structural highlights

Function

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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