View source for 3zlc


==Crystal Structure of Erv41p==
<StructureSection load='3zlc' size='340' side='right'caption='[[3zlc]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zlc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZLC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZLC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.999&#8491;</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=3zlc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zlc OCA], [https://pdbe.org/3zlc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zlc RCSB], [https://www.ebi.ac.uk/pdbsum/3zlc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zlc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ERV41_YEAST ERV41_YEAST] Constituent of COPII-coated endoplasmic reticulum-derived transport vesicles. Required for efficient transport of a subset of secretory proteins to the Golgi. The C-terminal Ile-Leu motif is required for exit from the endoplasmic reticulum. Facilitates retrograde transport from the Golgi to the endoplasmic reticulum.<ref>PMID:11157978</ref> <ref>PMID:12426381</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Erv41p is a conserved integral membrane protein that is known to play a role in transport between the endoplasmic reticulum and Golgi apparatus, part of the early secretory pathway of eukaryotes. However, the exact function of the protein is not known, and it shares very low sequence identity with proteins of known structure or function. Here we present the structure of the full lumenal domain of Erv41p from Saccharomyces cerevisiae, determined by X-ray crystallography to a resolution of 2.0A. The structure reveals the protein to be composed predominantly of two large beta-sheets that form a twisted beta-sandwich. Comparison to structures in the Protein Data Bank shows that the Erv41p lumenal domain displays only limited similarity to beta-sandwich domains of other proteins. Analysis of the surface properties of the protein identifies an extensive patch of negative electrostatic potential on the exposed surface of one of the beta-sheets, which likely forms a binding site for a ligand or interaction partner. A predominantly hydrophobic region close to the membrane interface is identified as a likely site for protein-protein interaction. This structure, the first of Erv41p or any of its homologues, provides a new starting point for studies of the roles of Erv41p and its interaction partners in the eukaryotic secretory pathway.

The Crystal Structure of the Lumenal Domain of Erv41p, a Protein Involved in Transport between the Endoplasmic Reticulum and Golgi Apparatus.,Biterova EI, Svard M, Possner DD, Guy JE J Mol Biol. 2013 Mar 21. pii: S0022-2836(13)00173-3. doi:, 10.1016/j.jmb.2013.03.024. PMID:23524136<ref>PMID:23524136</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zlc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Biterova EI]]
[[Category: Guy JE]]
[[Category: Possner DDD]]
[[Category: Svard M]]