6k9y: Difference between revisions
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==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]] | |||
