8xit: Difference between revisions
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==Cryo-EM structure of sheep VMAT2 dimer in an atypical fold== | |||
<StructureSection load='8xit' size='340' side='right'caption='[[8xit]], [[Resolution|resolution]] 3.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8xit]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8XIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XIT FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2Å</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=8xit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xit OCA], [https://pdbe.org/8xit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xit RCSB], [https://www.ebi.ac.uk/pdbsum/8xit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xit ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Vesicular monoamine transporter 2 (VMAT2) belongs to the major facilitator superfamily (MFS), and mediates cytoplasmic monoamine packaging into presynaptic vesicles. Here, we present two cryo-EM structures of VMAT2, with a frog VMAT2 adopting a canonical MFS fold and an engineered sheep VMAT2 adopting a non-canonical fold. Both VMAT2 proteins mediate uptake of a selective fluorescent VMAT2 substrate into cells. Molecular docking, substrate binding and transport analysis reveal potential substrate binding mechanism in VMAT2. Meanwhile, caution is advised when interpreting engineered membrane protein structures. | |||
Engineering of a mammalian VMAT2 for cryo-EM analysis results in non-canonical protein folding.,Lyu Y, Fu C, Ma H, Su Z, Sun Z, Zhou X Nat Commun. 2024 Aug 2;15(1):6511. doi: 10.1038/s41467-024-50934-5. PMID:39095428<ref>PMID:39095428</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8xit" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Ovis aries]] | |||
[[Category: Fu C]] | |||
[[Category: Lyu Y]] | |||
[[Category: Ma H]] | |||
[[Category: Su Z]] | |||
[[Category: Sun Z]] | |||
[[Category: Zhou X]] | |||
Latest revision as of 11:19, 14 August 2024
Cryo-EM structure of sheep VMAT2 dimer in an atypical foldCryo-EM structure of sheep VMAT2 dimer in an atypical fold
Structural highlights
Publication Abstract from PubMedVesicular monoamine transporter 2 (VMAT2) belongs to the major facilitator superfamily (MFS), and mediates cytoplasmic monoamine packaging into presynaptic vesicles. Here, we present two cryo-EM structures of VMAT2, with a frog VMAT2 adopting a canonical MFS fold and an engineered sheep VMAT2 adopting a non-canonical fold. Both VMAT2 proteins mediate uptake of a selective fluorescent VMAT2 substrate into cells. Molecular docking, substrate binding and transport analysis reveal potential substrate binding mechanism in VMAT2. Meanwhile, caution is advised when interpreting engineered membrane protein structures. Engineering of a mammalian VMAT2 for cryo-EM analysis results in non-canonical protein folding.,Lyu Y, Fu C, Ma H, Su Z, Sun Z, Zhou X Nat Commun. 2024 Aug 2;15(1):6511. doi: 10.1038/s41467-024-50934-5. PMID:39095428[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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