4tjv: Difference between revisions
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==Crystal structure of protease-associated domain of Arabidopsis vacuolar sorting receptor 1== | ==Crystal structure of protease-associated domain of Arabidopsis vacuolar sorting receptor 1== | ||
<StructureSection load='4tjv' size='340' side='right' caption='[[4tjv]], [[Resolution|resolution]] 1.65Å' scene=''> | <StructureSection load='4tjv' size='340' side='right'caption='[[4tjv]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4tjv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TJV OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4tjv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TJV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TJV FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.651Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4tjv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tjv OCA], [https://pdbe.org/4tjv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tjv RCSB], [https://www.ebi.ac.uk/pdbsum/4tjv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tjv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/VSR1_ARATH VSR1_ARATH] Vacuolar-sorting receptor (VSR) involved in clathrin-coated vesicles sorting from Golgi apparatus to vacuoles. Required for the sorting of 12S globulin, 2S albumin and maybe other seed storage proteins to protein storage vacuoles (PSVs) in seeds. May also be implicated in targeting N-terminal propeptide containing proteins to lytic vacuoles.<ref>PMID:10871276</ref> <ref>PMID:14657332</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4tjv" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Arabidopsis thaliana]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Fong YH]] | ||
[[Category: | [[Category: Jiang LW]] | ||
[[Category: | [[Category: Luo F]] | ||
[[Category: | [[Category: Wong KB]] | ||
Latest revision as of 03:46, 28 December 2023
Crystal structure of protease-associated domain of Arabidopsis vacuolar sorting receptor 1Crystal structure of protease-associated domain of Arabidopsis vacuolar sorting receptor 1
Structural highlights
FunctionVSR1_ARATH Vacuolar-sorting receptor (VSR) involved in clathrin-coated vesicles sorting from Golgi apparatus to vacuoles. Required for the sorting of 12S globulin, 2S albumin and maybe other seed storage proteins to protein storage vacuoles (PSVs) in seeds. May also be implicated in targeting N-terminal propeptide containing proteins to lytic vacuoles.[1] [2] Publication Abstract from PubMedIn plant cells, soluble proteins are directed to vacuoles because they contain vacuolar sorting determinants (VSDs) that are recognized by vacuolar sorting receptors (VSR). To understand how a VSR recognizes its cargo, we present the crystal structures of the protease-associated domain of VSR isoform 1 from Arabidopsis thaliana (VSR1PA) alone and complexed with a cognate peptide containing the barley (Hordeum vulgare) aleurain VSD sequence of 1ADSNPIRPVT10. The crystal structures show that VSR1PA binds the sequence, Ala-Asp-Ser, preceding the NPIR motif. A conserved cargo binding loop, with a consensus sequence of 95RGxCxF100, forms a cradle that accommodates the cargo-peptide. In particular, Arg-95 forms a hydrogen bond to the Ser-3 position of the VSD, and the essential role of Arg-95 and Ser-3 in receptor-cargo interaction was supported by a mutagenesis study. Cargo binding induces conformational changes that are propagated from the cargo binding loop to the C terminus via conserved residues in switch I-IV regions. The resulting 180 degrees swivel motion of the C-terminal tail is stabilized by a hydrogen bond between Glu-24 and His-181. A mutagenesis study showed that these two residues are essential for cargo interaction and trafficking. Based on our structural and functional studies, we present a model of how VSRs recognize their cargos. How vacuolar sorting receptor proteins interact with their cargo proteins: crystal structures of apo and cargo-bound forms of the protease-associated domain from an Arabidopsis vacuolar sorting receptor.,Luo F, Fong YH, Zeng Y, Shen J, Jiang L, Wong KB Plant Cell. 2014 Sep;26(9):3693-708. doi: 10.1105/tpc.114.129940. Epub 2014 Sep, 30. PMID:25271241[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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