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.
6k9y
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human VAT-1== | |
| + | <StructureSection load='6k9y' size='340' side='right'caption='[[6k9y]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6k9y]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K9Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6K9Y FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></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=6k9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k9y OCA], [http://pdbe.org/6k9y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k9y RCSB], [http://www.ebi.ac.uk/pdbsum/6k9y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k9y ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/VAT1_HUMAN VAT1_HUMAN]] Possesses ATPase activity (By similarity). Plays a part in calcium-regulated keratinocyte activation in epidermal repair mechanisms. Has no effect on cell proliferation. Negatively regulates mitochondrial fusion in cooperation with mitofusin proteins (MFN1-2).<ref>PMID:12898150</ref> <ref>PMID:17105775</ref> <ref>PMID:19508442</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Eukaryotic cells are compartmentalized to form organelles, whose functions rely on proper phospholipid and protein transport. Here we determined the crystal structure of human VAT-1, a cytosolic soluble protein that was suggested to transfer phosphatidylserine, at 2.2 A resolution. We found that VAT-1 transferred not only phosphatidylserine but also other acidic phospholipids between membranes in vitro. Structure-based mutational analyses showed the presence of a possible lipid-binding cavity at the interface between the two sub-domains, and two tyrosine residues in the flexible loops facilitated phospholipid transfer, likely by functioning as a gate to this lipid-binding cavity. We also found that a basic and hydrophobic loop with two tryptophan residues was protruded from the molecule and facilitated binding to the acidic-lipid membranes, thereby achieving efficient phospholipid transfer. | ||
| - | + | Structural basis for inter-organelle phospholipid transport mediated by VAT-1.,Watanabe Y, Tamura Y, Kakuta C, Watanabe S, Endo T J Biol Chem. 2020 Jan 31. pii: RA119.011019. doi: 10.1074/jbc.RA119.011019. PMID:32005660<ref>PMID:32005660</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6k9y" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Endo, T]] | ||
| + | [[Category: Watanabe, Y]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Phospholipid transfer protein]] | ||
Revision as of 04:11, 13 February 2020
Crystal structure of human VAT-1
| |||||||||||
