4in3

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'''Unreleased structure'''
 
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The entry 4in3 is ON HOLD until Paper Publication
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==Crystal Structure of the Chs5-Bch1 Exomer Cargo Adaptor Complex==
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<StructureSection load='4in3' size='340' side='right'caption='[[4in3]], [[Resolution|resolution]] 2.94&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4in3]] is a 4 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=4IN3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IN3 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.936&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4in3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4in3 OCA], [https://pdbe.org/4in3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4in3 RCSB], [https://www.ebi.ac.uk/pdbsum/4in3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4in3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Exomer is a cargo adaptor that mediates the sorting of specific plasma membrane proteins into vesicles at the trans-Golgi network. Cargo adaptors must bind to multiple partners, including their cargo, regulatory proteins, and the membrane surface. During biogenesis of a vesicle, the membrane makes a transition from a relatively flat surface to one of high curvature, requiring cargo adaptors to somehow maintain protein-protein and protein-membrane interactions on a changing membrane environment. Here, we present the crystal structure of a tetrameric Chs5/Bch1 exomer complex and use small-angle X-ray scattering to demonstrate its flexibility in solution. The structural data suggest that the complex flexes primarily around the dimeric N-terminal domain of the Chs5 subunits, which adopts a noncanonical beta sandwich fold. We propose that this flexible hinge domain enables exomer to maintain interactions in the context of a dynamic membrane environment.
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Authors: Richardson, B.C., Fromme, J.C.
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The Exomer Cargo Adaptor Features a Flexible Hinge Domain.,Richardson BC, Fromme JC Structure. 2013 Feb 5. pii: S0969-2126(13)00006-3. doi:, 10.1016/j.str.2013.01.003. PMID:23395181<ref>PMID:23395181</ref>
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Description: Crystal Structure of the Chs5-Bch1 Exomer Cargo Adaptor Complex
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4in3" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Fromme JC]]
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[[Category: Richardson BC]]

Current revision

Crystal Structure of the Chs5-Bch1 Exomer Cargo Adaptor Complex

PDB ID 4in3

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