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6k9y

From Proteopedia

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Crystal structure of human VAT-1

Structural highlights

6k9y is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).^[1] ^[2] ^[3]

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Koch J, Foekens J, Timmermans M, Fink W, Wirzbach A, Kramer MD, Schaefer BM. Human VAT-1: a calcium-regulated activation marker of human epithelial cells. Arch Dermatol Res. 2003 Sep;295(5):203-10. doi: 10.1007/s00403-003-0421-8. Epub, 2003 Jul 30. PMID:12898150 doi:http://dx.doi.org/10.1007/s00403-003-0421-8
↑ Eura Y, Ishihara N, Oka T, Mihara K. Identification of a novel protein that regulates mitochondrial fusion by modulating mitofusin (Mfn) protein function. J Cell Sci. 2006 Dec 1;119(Pt 23):4913-25. doi: 10.1242/jcs.03253. Epub 2006 Nov , 14. PMID:17105775 doi:http://dx.doi.org/10.1242/jcs.03253
↑ Mertsch S, Becker M, Lichota A, Paulus W, Senner V. Vesicle amine transport protein-1 (VAT-1) is upregulated in glioblastomas and promotes migration. Neuropathol Appl Neurobiol. 2009 Aug;35(4):342-52. doi:, 10.1111/j.1365-2990.2009.00993.x. PMID:19508442 doi:http://dx.doi.org/10.1111/j.1365-2990.2009.00993.x
↑ Watanabe Y, Tamura Y, Kakuta C, Watanabe S, Endo T. Structural basis for inter-organelle phospholipid transport mediated by VAT-1. J Biol Chem. 2020 Jan 31. pii: RA119.011019. doi: 10.1074/jbc.RA119.011019. PMID:32005660 doi:http://dx.doi.org/10.1074/jbc.RA119.011019

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/6k9y"

Categories: Homo sapiens | Large Structures | Endo T | Watanabe Y

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6k9y is ON HOLD
+==Crystal structure of human VAT-1==
+<StructureSection load='6k9y' size='340' side='right'caption='[[6k9y]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6k9y]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6K9Y 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]] 2.2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=6k9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k9y OCA], [https://pdbe.org/6k9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k9y RCSB], [https://www.ebi.ac.uk/pdbsum/6k9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k9y ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6k9y" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Endo T]]
+[[Category: Watanabe Y]]

6k9y

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Current revision

Crystal structure of human VAT-1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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