View source for 4yg8


==CRYSTAL STRUCTURE OF THE CHS5-CHS6 EXOMER CARGO ADAPTOR COMPLEX==
<StructureSection load='4yg8' size='340' side='right'caption='[[4yg8]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4yg8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4gns 4gns]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YG8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YG8 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=4yg8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yg8 OCA], [https://pdbe.org/4yg8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yg8 RCSB], [https://www.ebi.ac.uk/pdbsum/4yg8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yg8 ProSAT]</span></td></tr>
</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 ==
Cargo adaptors control intracellular trafficking of transmembrane proteins by sorting them into membrane transport carriers. The COPI, COPII, and clathrin cargo adaptors are structurally well characterized, but other cargo adaptors remain poorly understood. Exomer is a specialized cargo adaptor that sorts specific proteins into trans-Golgi network (TGN)-derived vesicles in response to cellular signals. Exomer is recruited to the TGN by the Arf1 GTPase, a universally conserved trafficking regulator. Here, we report the crystal structure of a tetrameric exomer complex composed of two copies each of the Chs5 and Chs6 subunits. The structure reveals the FN3 and BRCT domains of Chs5, which together we refer to as the FBE domain (FN3-BRCT of exomer), project from the exomer core complex. The overall architecture of the FBE domain is reminiscent of the appendage domains of other cargo adaptors, although it exhibits a distinct topology. In contrast to appendage domains, which bind accessory factors, we show that the primary role of the FBE domain is to bind Arf1 for recruitment of exomer to membranes.

The exomer cargo adaptor structure reveals a novel GTPase-binding domain.,Paczkowski JE, Richardson BC, Strassner AM, Fromme JC EMBO J. 2012 Sep 21. doi: 10.1038/emboj.2012.268. PMID:23000721<ref>PMID:23000721</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4yg8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Fromme JC]]
[[Category: Paczkowski JE]]
[[Category: Richardson BC]]
[[Category: Strassner AM]]