|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Solution structure of Saccharomyces cerevisiae conserved oligomeric Golgi subunit 2 protein (Cog2p)== | | ==Solution structure of Saccharomyces cerevisiae conserved oligomeric Golgi subunit 2 protein (Cog2p)== |
| - | <StructureSection load='2jqq' size='340' side='right'caption='[[2jqq]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2jqq' size='340' side='right'caption='[[2jqq]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jqq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JQQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JQQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jqq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JQQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JQQ FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">COG2, SEC35 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | + | </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=2jqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jqq OCA], [https://pdbe.org/2jqq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jqq RCSB], [https://www.ebi.ac.uk/pdbsum/2jqq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jqq ProSAT]</span></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=2jqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jqq OCA], [https://pdbe.org/2jqq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jqq RCSB], [https://www.ebi.ac.uk/pdbsum/2jqq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jqq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/COG2_YEAST COG2_YEAST]] Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events. COG2 is required for ER to Golgi vesicle docking. Not essential for viability.<ref>PMID:9606204</ref> <ref>PMID:12006647</ref>
| + | [https://www.uniprot.org/uniprot/COG2_YEAST COG2_YEAST] Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events. COG2 is required for ER to Golgi vesicle docking. Not essential for viability.<ref>PMID:9606204</ref> <ref>PMID:12006647</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 22: |
Line 21: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cavanaugh, L F]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Chen, X]] | + | [[Category: Cavanaugh LF]] |
| - | [[Category: Hughson, F M]] | + | [[Category: Chen X]] |
| - | [[Category: Pelczer, I]] | + | [[Category: Hughson FM]] |
| - | [[Category: Rizo, J]] | + | [[Category: Pelczer I]] |
| - | [[Category: Helical bundle]]
| + | [[Category: Rizo J]] |
| - | [[Category: Protein]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Tethering]]
| + | |
| - | [[Category: Vesicular transport]]
| + | |
| Structural highlights
Function
COG2_YEAST Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events. COG2 is required for ER to Golgi vesicle docking. Not essential for viability.[1] [2]
Publication Abstract from PubMed
The conserved oligomeric Golgi (COG) complex is strongly implicated in retrograde vesicular trafficking within the Golgi apparatus. Although its mechanism of action is poorly understood, it has been proposed to function by mediating the initial physical contact between transport vesicles and their membrane targets. An analogous role in tethering vesicles has been suggested for at least six additional large multisubunit complexes, including the exocyst, a complex essential for trafficking to the plasma membrane. Here we report the solution structure of a large portion of yeast Cog2p, one of eight subunits composing the COG complex. The structure reveals a six-helix bundle with few conserved surface features but a general resemblance to recently determined crystal structures of four different exocyst subunits. This finding provides the first structural evidence that COG, like the exocyst and potentially other tethering complexes, is constructed from helical bundles. These structures may represent platforms for interaction with other trafficking proteins including SNAREs (soluble N-ethylmaleimide factor attachment protein receptors) and Rabs.
Structural analysis of conserved oligomeric Golgi complex subunit 2.,Cavanaugh LF, Chen X, Richardson BC, Ungar D, Pelczer I, Rizo J, Hughson FM J Biol Chem. 2007 Aug 10;282(32):23418-26. Epub 2007 Jun 12. PMID:17565980[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ VanRheenen SM, Cao X, Lupashin VV, Barlowe C, Waters MG. Sec35p, a novel peripheral membrane protein, is required for ER to Golgi vesicle docking. J Cell Biol. 1998 Jun 1;141(5):1107-19. PMID:9606204
- ↑ Ram RJ, Li B, Kaiser CA. Identification of Sec36p, Sec37p, and Sec38p: components of yeast complex that contains Sec34p and Sec35p. Mol Biol Cell. 2002 May;13(5):1484-500. PMID:12006647 doi:http://dx.doi.org/10.1091/mbc.01-10-0495
- ↑ Cavanaugh LF, Chen X, Richardson BC, Ungar D, Pelczer I, Rizo J, Hughson FM. Structural analysis of conserved oligomeric Golgi complex subunit 2. J Biol Chem. 2007 Aug 10;282(32):23418-26. Epub 2007 Jun 12. PMID:17565980 doi:http://dx.doi.org/M703716200
|
