3onj

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of yeast Vti1p_Habc domain

Structural highlights

3onj is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.92Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VTI1_YEAST t-SNARE found in various SNARE complexes involved in multiple transport pathways. The composition of the t-SNARE complexes is specific for a limited number of v-SNAREs and therefore allows only the vesicles carrying the matching v-SNARE to fuse.^[1] ^[2] ^[3]

Publication Abstract from PubMed

SNARE proteins are crucial for membrane fusion in vesicular transport. To ensure efficient and accurate fusion, SNAREs need to be sorted into different budding vesicles. This process is usually regulated by specific recognition between SNAREs and their adaptor proteins. How different pairs of SNAREs and adaptors achieve their recognition is unclear. Here, we report the recognition between yeast SNARE Vti1p and its adaptor Ent3p derived from three crystal structures. Surprisingly, this yeast pair Vti1p/Ent3p interacts through a distinct binding site compared to their homologues vti1b/epsinR in mammals. An opposite surface on Vti1p_Habc domain binds to a conserved area on the epsin N-terminal homology (ENTH) domain of Ent3p. Two-hybrid, in vitro pull-down and in vivo experiments indicate this binding interface is important for correct localization of Vti1p in the cell. This previously undescribed discovery that a cargo and adaptor pair uses different binding sites across species suggests the diversity of SNARE-adaptor recognition in vesicular transport.

Epsin N-terminal homology domains bind on opposite sides of two SNAREs.,Wang J, Gossing M, Fang P, Zimmermann J, Li X, von Mollard GF, Niu L, Teng M Proc Natl Acad Sci U S A. 2011 Jul 26;108(30):12277-82. Epub 2011 Jul 11. PMID:21746902^[4]

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
↑ Paumet F, Brugger B, Parlati F, McNew JA, Sollner TH, Rothman JE. A t-SNARE of the endocytic pathway must be activated for fusion. J Cell Biol. 2001 Dec 10;155(6):961-8. Epub 2001 Dec 10. PMID:11739407 doi:http://dx.doi.org/10.1083/jcb.200104092
↑ Paumet F, Rahimian V, Rothman JE. The specificity of SNARE-dependent fusion is encoded in the SNARE motif. Proc Natl Acad Sci U S A. 2004 Mar 9;101(10):3376-80. Epub 2004 Feb 23. PMID:14981247 doi:http://dx.doi.org/10.1073/pnas.0400271101
↑ Wang J, Gossing M, Fang P, Zimmermann J, Li X, von Mollard GF, Niu L, Teng M. Epsin N-terminal homology domains bind on opposite sides of two SNAREs. Proc Natl Acad Sci U S A. 2011 Jul 26;108(30):12277-82. Epub 2011 Jul 11. PMID:21746902 doi:10.1073/pnas.1013101108

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/3onj"

@@ Line 1: / Line 1: @@
-[[Image:3onj.png|left|200px]]
-<!--
+==Crystal structure of yeast Vti1p_Habc domain==
-The line below this paragraph, containing "STRUCTURE_3onj", creates the "Structure Box" on the page.
+<StructureSection load='3onj' size='340' side='right'caption='[[3onj]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3onj]] is a 1 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=3ONJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ONJ FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.92&#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=3onj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3onj OCA], [https://pdbe.org/3onj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3onj RCSB], [https://www.ebi.ac.uk/pdbsum/3onj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3onj ProSAT]</span></td></tr>
-{{STRUCTURE_3onj|  PDB=3onj  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/VTI1_YEAST VTI1_YEAST] t-SNARE found in various SNARE complexes involved in multiple transport pathways. The composition of the t-SNARE complexes is specific for a limited number of v-SNAREs and therefore allows only the vesicles carrying the matching v-SNARE to fuse.<ref>PMID:10385523</ref> <ref>PMID:11739407</ref> <ref>PMID:14981247</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+SNARE proteins are crucial for membrane fusion in vesicular transport. To ensure efficient and accurate fusion, SNAREs need to be sorted into different budding vesicles. This process is usually regulated by specific recognition between SNAREs and their adaptor proteins. How different pairs of SNAREs and adaptors achieve their recognition is unclear. Here, we report the recognition between yeast SNARE Vti1p and its adaptor Ent3p derived from three crystal structures. Surprisingly, this yeast pair Vti1p/Ent3p interacts through a distinct binding site compared to their homologues vti1b/epsinR in mammals. An opposite surface on Vti1p_Habc domain binds to a conserved area on the epsin N-terminal homology (ENTH) domain of Ent3p. Two-hybrid, in vitro pull-down and in vivo experiments indicate this binding interface is important for correct localization of Vti1p in the cell. This previously undescribed discovery that a cargo and adaptor pair uses different binding sites across species suggests the diversity of SNARE-adaptor recognition in vesicular transport.
-===Crystal structure of yeast Vti1p_Habc domain===
+Epsin N-terminal homology domains bind on opposite sides of two SNAREs.,Wang J, Gossing M, Fang P, Zimmermann J, Li X, von Mollard GF, Niu L, Teng M Proc Natl Acad Sci U S A. 2011 Jul 26;108(30):12277-82. Epub 2011 Jul 11. PMID:21746902<ref>PMID:21746902</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-==About this Structure==
+</div>
-[[3onj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ONJ OCA].
+<div class="pdbe-citations 3onj" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Fang, P.]]
+[[Category: Fang P]]
-[[Category: Niu, L.]]
+[[Category: Niu L]]
-[[Category: Teng, M.]]
+[[Category: Teng M]]
-[[Category: Wang, J.]]
+[[Category: Wang J]]
-[[Category: Habc]]
-[[Category: Helix]]
-[[Category: Protein transport]]

3onj

From Proteopedia

Current revision

Crystal structure of yeast Vti1p_Habc domain

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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