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6q0x

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'''Unreleased structure'''
 
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The entry 6q0x is ON HOLD until Paper Publication
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==The cryo-EM structure of the SNX-BAR Mvp1 tetramer==
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<StructureSection load='6q0x' size='340' side='right'caption='[[6q0x]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6q0x]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q0X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q0X FirstGlance]. <br>
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</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=6q0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q0x OCA], [http://pdbe.org/6q0x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q0x RCSB], [http://www.ebi.ac.uk/pdbsum/6q0x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q0x ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/MVP1_YEAST MVP1_YEAST]] Required for vacuolar protein sorting.<ref>PMID:7862158</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Sorting nexins (SNX) are a family of PX domain-containing proteins with pivotal roles in trafficking and signaling. SNX-BARs, which also have a curvature-generating Bin/Amphiphysin/Rvs (BAR) domain, have membrane-remodeling functions, particularly at the endosome. The minimal PX-BAR module is a dimer mediated by BAR-BAR interactions. Many SNX-BAR proteins, however, additionally have low-complexity N-terminal regions of unknown function. Here, we present the cryo-EM structure of the full-length SNX-BAR Mvp1, which is an autoinhibited tetramer. The tetramer is a dimer of dimers, wherein the membrane-interacting BAR surfaces are sequestered and the PX lipid-binding sites are occluded. The N-terminal low-complexity region of Mvp1 is essential for tetramerization. Mvp1 lacking its N-terminus is dimeric and exhibits enhanced membrane association. Membrane binding and remodeling by Mvp1 therefore requires unmasking of the PX and BAR domain lipid-interacting surfaces. This work reveals a tetrameric configuration of a SNX-BAR protein that provides critical insight into SNX-BAR function and regulation.
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Authors:
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The cryo-EM structure of the SNX-BAR Mvp1 tetramer.,Sun D, Varlakhanova NV, Tornabene BA, Ramachandran R, Zhang P, Ford MGJ Nat Commun. 2020 Mar 20;11(1):1506. doi: 10.1038/s41467-020-15110-5. PMID:32198400<ref>PMID:32198400</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6q0x" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Ford, M G.J]]
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[[Category: Sun, D]]
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[[Category: Zhang, P]]
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[[Category: Bar]]
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[[Category: Lipid binding protein]]
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[[Category: Mvp1]]
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[[Category: Px]]
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[[Category: Snx]]
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[[Category: Snx-bar]]
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[[Category: Sorting nexin]]

Revision as of 09:16, 1 April 2020

The cryo-EM structure of the SNX-BAR Mvp1 tetramer

PDB ID 6q0x

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