4wjw
From Proteopedia
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==Crystal Structure of the Chs5-Chs6 Exomer Cargo Adaptor Complex Bound to portion of Chs3== | ==Crystal Structure of the Chs5-Chs6 Exomer Cargo Adaptor Complex Bound to portion of Chs3== | ||
| - | <StructureSection load='4wjw' size='340' side='right' caption='[[4wjw]], [[Resolution|resolution]] 2.59Å' scene=''> | + | <StructureSection load='4wjw' size='340' side='right'caption='[[4wjw]], [[Resolution|resolution]] 2.59Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4wjw]] is a 3 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4u9t 4u9t]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WJW OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[4wjw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4u9t 4u9t]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WJW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WJW FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.59Å</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=4wjw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wjw OCA], [https://pdbe.org/4wjw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wjw RCSB], [https://www.ebi.ac.uk/pdbsum/4wjw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wjw ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CHS5_YEAST CHS5_YEAST] Component of the CHS5/6 complex which mediates export of specific cargo proteins, including chitin synthase CHS3. Also involved in targeting FUS1 to sites of polarized growth.<ref>PMID:9111317</ref> <ref>PMID:8197125</ref> <ref>PMID:12912901</ref> <ref>PMID:15715908</ref> <ref>PMID:16498409</ref> <ref>PMID:16818716</ref> <ref>PMID:17000877</ref> <ref>PMID:16855022</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cells transport integral membrane proteins between organelles by sorting them into vesicles. Cargo adaptors act to recognize sorting signals in transmembrane cargos and to interact with coat complexes that aid in vesicle biogenesis. No coat proteins have yet been identified that generate secretory vesicles from the trans-Golgi network (TGN) to the plasma membrane, but the exomer complex has been identified as a cargo adaptor complex that mediates transport of several proteins in this pathway. Chs3, the most well-studied exomer cargo, cycles between the TGN and the plasma membrane in synchrony with the cell cycle, providing an opportunity to study regulation of proteins that cycle in response to signaling. Here we show that different segments of the Chs3 N-terminus mediate distinct trafficking steps. Residues 10-27, known to mediate retention, also appear to play a role in internalization. Residues 28-52 are involved in transport to the plasma membrane and recycling out of endosomes to prevent degradation in the vacuole. We also present the crystal structure of residues 10-27 bound to the exomer complex, suggesting different cargo adaptors could compete for binding to this segment, providing a potential mechanism for regulation. | ||
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| + | Distinct N-terminal regions of the exomer secretory vesicle cargo Chs3 regulate its trafficking itinerary.,Weiskoff AM, Fromme JC Front Cell Dev Biol. 2014 Sep 3;2:47. doi: 10.3389/fcell.2014.00047. eCollection , 2014. PMID:25364754<ref>PMID:25364754</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4wjw" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: | + | [[Category: Fromme JC]] |
| - | [[Category: | + | [[Category: Weiskoff AM]] |
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Current revision
Crystal Structure of the Chs5-Chs6 Exomer Cargo Adaptor Complex Bound to portion of Chs3
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