View source for 6lhr


==Crystal structure of the complex between Vesicle Amine Transport-1 and NADP==
<StructureSection load='6lhr' size='340' side='right'caption='[[6lhr]], [[Resolution|resolution]] 2.62&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6lhr]] 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=6LHR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LHR 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]] 2.62&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=6lhr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lhr OCA], [https://pdbe.org/6lhr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lhr RCSB], [https://www.ebi.ac.uk/pdbsum/6lhr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lhr 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 ==
Vesicle amine transport protein-1 (VAT-1) has been implicated in the regulation of vesicular transport, mitochondrial fusion, phospholipid transport and cell migration, and is a potential target of anticancer drugs. Little is known about the molecular function of VAT-1. The amino acid sequence indicates that VAT-1 belongs to the quinone oxidoreductase subfamily, suggesting that VAT-1 may possess enzymatic activity in unknown redox processes. To clarify the molecular function of VAT-1, we determined the three-dimensional structure of human VAT-1 in the free state at 2.3 A resolution and found that VAT-1 forms a dimer with the conserved NADPH-binding cleft on each protomer. We also determined the structure of VAT-1 in the NADP-bound state at 2.6 A resolution and found that NADP binds the binding cleft to create a putative active site with the nicotine ring. Substrate screening suggested that VAT-1 possesses oxidoreductase activity against quinones such as 1,2-naphthoquinone and 9,10-phenanthrenequinone.

Structural insights into vesicle amine transport-1 (VAT-1) as a member of the NADPH-dependent quinone oxidoreductase family.,Kim SY, Mori T, Chek MF, Furuya S, Matsumoto K, Yajima T, Ogura T, Hakoshima T Sci Rep. 2021 Jan 22;11(1):2120. doi: 10.1038/s41598-021-81409-y. PMID:33483563<ref>PMID:33483563</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6lhr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Hakoshima T]]
[[Category: Kim S-Y]]
[[Category: Mori T]]