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6lii
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==A quinone oxidoreductase== | |
| + | <StructureSection load='6lii' size='340' side='right'caption='[[6lii]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6lii]] 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=6LII OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LII 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]] 2.3Å</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=6lii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lii OCA], [https://pdbe.org/6lii PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lii RCSB], [https://www.ebi.ac.uk/pdbsum/6lii PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lii 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Hakoshima | + | <div class="pdbe-citations 6lii" style="background-color:#fffaf0;"></div> |
| - | [[Category: Kim | + | == References == |
| - | [[Category: Mori | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Hakoshima T]] | ||
| + | [[Category: Kim S-Y]] | ||
| + | [[Category: Mori T]] | ||
Current revision
A quinone oxidoreductase
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