View source for 2fz0


==Identification of yeast R-SNARE Nyv1p as a novel longin domain protein==
<StructureSection load='2fz0' size='340' side='right'caption='[[2fz0]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2fz0]] 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=2FZ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FZ0 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2fz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fz0 OCA], [https://pdbe.org/2fz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fz0 RCSB], [https://www.ebi.ac.uk/pdbsum/2fz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fz0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NYV1_YEAST NYV1_YEAST] Vacuolar v-SNARE required for docking. Only involved in homotypic vacuole fusion. Required for Ca(2+) efflux from the vacuolar lumen, a required signal for subsequent membrane fusion events, by inhibiting vacuolar Ca(2+)-ATPase PMC1 and promoting Ca(2+) release when forming trans-SNARE assemblies during the docking step.<ref>PMID:10385523</ref> <ref>PMID:11080502</ref> <ref>PMID:14734531</ref> <ref>PMID:9144293</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Using nuclear magnetic resonance spectroscopy, we establish that the N-terminal domain of the yeast vacuolar R-SNARE Nyv1p adopts a longin-like fold similar to those of Sec22b and Ykt6p. Nyv1p is sorted to the limiting membrane of the vacuole via the adaptor protein (AP)3 adaptin pathway, and we show that its longin domain is sufficient to direct transport to this location. In contrast, we found that the longin domains of Sec22p and Ykt6p were not sufficient to direct their localization. A YXX phi-like adaptin-dependent sorting signal (Y31GTI34) unique to the longin domain of Nyv1p mediates interactions with the AP3 complex in vivo and in vitro. We show that amino acid substitutions to Y31GTI34 (Y31Q;I34Q) resulted in mislocalization of Nyv1p as well as reduced binding of the mutant protein to the AP3 complex. Although the sorting of Nyv1p to the limiting membrane of the vacuole is dependent upon the Y31GTI34 motif, and Y31 in particular, our findings with structure-based amino acid substitutions in the mu chain (Apm3p) of yeast AP3 suggest a mechanistically distinct role for this subunit in the recognition of YXX phi-like sorting signals.

Identification of the yeast R-SNARE Nyv1p as a novel longin domain-containing protein.,Wen W, Chen L, Wu H, Sun X, Zhang M, Banfield DK Mol Biol Cell. 2006 Oct;17(10):4282-99. Epub 2006 Jul 19. PMID:16855025<ref>PMID:16855025</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2fz0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Wen W]]
[[Category: Zhang M]]