3vp7

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m (Protected "3vp7" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 3vp7 is ON HOLD
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==Crystal structure of the beta-alpha repeated, autophagy-specific (BARA) domain of Vps30/Atg6==
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<StructureSection load='3vp7' size='340' side='right'caption='[[3vp7]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3vp7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VP7 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vp7 OCA], [https://pdbe.org/3vp7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vp7 RCSB], [https://www.ebi.ac.uk/pdbsum/3vp7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vp7 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BECN1_YEAST BECN1_YEAST] Required for cytoplasm to vacuole transport (Cvt), autophagy, nucleophagy, and mitophagy, as a part of the autophagy-specific VPS34 PI3-kinase complex I. This complex is essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). Plays also a role in regulation of filamentous growth.<ref>PMID:11157979</ref> <ref>PMID:11689437</ref> <ref>PMID:12244127</ref> <ref>PMID:16267277</ref> <ref>PMID:17404498</ref> <ref>PMID:17700056</ref> <ref>PMID:18182384</ref> <ref>PMID:18701704</ref> <ref>PMID:19131141</ref> <ref>PMID:22437838</ref> <ref>PMID:23878393</ref> <ref>PMID:8224160</ref> <ref>PMID:9105038</ref> <ref>PMID:9712845</ref>
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Authors: Noda, N.N., Kobayashi, T., Adachi, W., Fujioka, Y., Ohsumi, Y., Inagaki, F.
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==See Also==
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*[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]]
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Description: Crystal structure of the beta-alpha repeated, autophagy-specific (BARA) domain of Vps30/Atg6
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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: Saccharomyces cerevisiae S288C]]
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[[Category: Adachi W]]
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[[Category: Fujioka Y]]
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[[Category: Inagaki F]]
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[[Category: Kobayashi T]]
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[[Category: Noda NN]]
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[[Category: Ohsumi Y]]

Current revision

Crystal structure of the beta-alpha repeated, autophagy-specific (BARA) domain of Vps30/Atg6

PDB ID 3vp7

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