3onj: Difference between revisions
New page: '''Unreleased structure''' The entry 3onj is ON HOLD Authors: Wang, J., Fang, P., Niu, L., Teng, M. Description: crystal structure of yeast Vti1p Habc domain ''Page seeded by [http://... |
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The | ==Crystal structure of yeast Vti1p_Habc domain== | ||
<StructureSection load='3onj' size='340' side='right'caption='[[3onj]], [[Resolution|resolution]] 1.92Å' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.92Å</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> | |||
</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. | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3onj" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae]] | |||
[[Category: Fang P]] | |||
[[Category: Niu L]] | |||
[[Category: Teng M]] | |||
[[Category: Wang J]] | |||
Latest revision as of 19:56, 1 November 2023
Crystal structure of yeast Vti1p_Habc domainCrystal structure of yeast Vti1p_Habc domain
Structural highlights
FunctionVTI1_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 PubMedSNARE 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
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