This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2fz0

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 12:59, 25 December 2014

Identification of yeast R-SNARE Nyv1p as a novel longin domain protein

Structural highlights

2fz0 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[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.^[1] ^[2] ^[3] ^[4]

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^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ungermann C, von Mollard GF, Jensen ON, Margolis N, Stevens TH, Wickner W. Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion. J Cell Biol. 1999 Jun 28;145(7):1435-42. PMID:10385523
↑ Takita Y, Engstrom L, Ungermann C, Cunningham KW. Inhibition of the Ca(2+)-ATPase Pmc1p by the v-SNARE protein Nyv1p. J Biol Chem. 2001 Mar 2;276(9):6200-6. Epub 2000 Nov 15. PMID:11080502 doi:http://dx.doi.org/10.1074/jbc.M009191200
↑ Merz AJ, Wickner WT. Trans-SNARE interactions elicit Ca2+ efflux from the yeast vacuole lumen. J Cell Biol. 2004 Jan 19;164(2):195-206. PMID:14734531 doi:http://dx.doi.org/10.1083/jcb.200310105
↑ Nichols BJ, Ungermann C, Pelham HR, Wickner WT, Haas A. Homotypic vacuolar fusion mediated by t- and v-SNAREs. Nature. 1997 May 8;387(6629):199-202. PMID:9144293 doi:http://dx.doi.org/10.1038/387199a0
↑ Wen W, Chen L, Wu H, Sun X, Zhang M, Banfield DK. Identification of the yeast R-SNARE Nyv1p as a novel longin domain-containing protein. Mol Biol Cell. 2006 Oct;17(10):4282-99. Epub 2006 Jul 19. PMID:16855025 doi:http://dx.doi.org/E06-02-0128

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2fz0"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fz0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fz0 RCSB], [http://www.ebi.ac.uk/pdbsum/2fz0 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://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 ==
@@ Line 18: / Line 20: @@
 </StructureSection>
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Wen, W.]]
+[[Category: Wen, W]]
-[[Category: Zhang, M.]]
+[[Category: Zhang, M]]
 [[Category: Longin domain]]
 [[Category: Membrane protein]]
 [[Category: Snare protein]]

2fz0

From Proteopedia

Revision as of 12:59, 25 December 2014

Identification of yeast R-SNARE Nyv1p as a novel longin domain protein

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox