6sur: Difference between revisions
New page: '''Unreleased structure''' The entry 6sur is ON HOLD Authors: Description: Category: Unreleased Structures |
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The | ==The Rab33B-Atg16L1 crystal structure== | ||
<StructureSection load='6sur' size='340' side='right'caption='[[6sur]], [[Resolution|resolution]] 3.47Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6sur]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SUR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SUR 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]] 3.467Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6sur FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sur OCA], [https://pdbe.org/6sur PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sur RCSB], [https://www.ebi.ac.uk/pdbsum/6sur PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sur ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RB33B_MOUSE RB33B_MOUSE] Protein transport. Acts, in coordination with RAB6A, to regulate intra-Golgi retrograde trafficking (By similarity). It is involved in autophagy, acting as a modulator of autophagosome formation.<ref>PMID:18448665</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Atg12-Atg5/Atg16L1 complex is recruited by WIPI2b to the site of autophagosome formation. Atg16L1 is an effector of the Golgi resident GTPase Rab33B. Here we identified a minimal stable complex of murine Rab33B(30-202) Q92L and Atg16L1(153-210). Atg16L1(153-210) comprises the C-terminal part of the Atg16L1 coiled-coil domain. We have determined the crystal structure of the Rab33B Q92L/Atg16L1(153-210) effector complex at 3.47 A resolution. This structure reveals that two Rab33B molecules bind to the diverging alpha-helices of the dimeric Atg16L1 coiled-coil domain. We mutated Atg16L1 and Rab33B interface residues and found that they disrupt complex formation in pull-down assays and cellular co-localization studies. The Rab33B binding site of Atg16L1 comprises 20 residues and immediately precedes the WIPI2b binding site. Rab33B mutations that abolish Atg16L binding also abrogate Rab33B association with the Golgi stacks. Atg16L1 mutants that are defective in Rab33B binding still co-localize with WIPI2b in vivo. The close proximity of the Rab33B and WIPI2b binding sites might facilitate the recruitment of Rab33B containing vesicles to provide a source of lipids during autophagosome biogenesis. | |||
Crystal structure of the Rab33B/Atg16L1 effector complex.,Metje-Sprink J, Groffmann J, Neumann P, Barg-Kues B, Ficner R, Kuhnel K, Schalk AM, Binotti B Sci Rep. 2020 Jul 31;10(1):12956. doi: 10.1038/s41598-020-69637-0. PMID:32737358<ref>PMID:32737358</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6sur" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Autophagy-related protein 3D structures|Autophagy-related protein 3D structures]] | |||
*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]] | |||
*[[Ras-related protein Rab 3D structures|Ras-related protein Rab 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Kuehnel K]] | |||
[[Category: Metje-Sprink J]] | |||
Latest revision as of 15:48, 24 January 2024
The Rab33B-Atg16L1 crystal structureThe Rab33B-Atg16L1 crystal structure
Structural highlights
FunctionRB33B_MOUSE Protein transport. Acts, in coordination with RAB6A, to regulate intra-Golgi retrograde trafficking (By similarity). It is involved in autophagy, acting as a modulator of autophagosome formation.[1] Publication Abstract from PubMedThe Atg12-Atg5/Atg16L1 complex is recruited by WIPI2b to the site of autophagosome formation. Atg16L1 is an effector of the Golgi resident GTPase Rab33B. Here we identified a minimal stable complex of murine Rab33B(30-202) Q92L and Atg16L1(153-210). Atg16L1(153-210) comprises the C-terminal part of the Atg16L1 coiled-coil domain. We have determined the crystal structure of the Rab33B Q92L/Atg16L1(153-210) effector complex at 3.47 A resolution. This structure reveals that two Rab33B molecules bind to the diverging alpha-helices of the dimeric Atg16L1 coiled-coil domain. We mutated Atg16L1 and Rab33B interface residues and found that they disrupt complex formation in pull-down assays and cellular co-localization studies. The Rab33B binding site of Atg16L1 comprises 20 residues and immediately precedes the WIPI2b binding site. Rab33B mutations that abolish Atg16L binding also abrogate Rab33B association with the Golgi stacks. Atg16L1 mutants that are defective in Rab33B binding still co-localize with WIPI2b in vivo. The close proximity of the Rab33B and WIPI2b binding sites might facilitate the recruitment of Rab33B containing vesicles to provide a source of lipids during autophagosome biogenesis. Crystal structure of the Rab33B/Atg16L1 effector complex.,Metje-Sprink J, Groffmann J, Neumann P, Barg-Kues B, Ficner R, Kuhnel K, Schalk AM, Binotti B Sci Rep. 2020 Jul 31;10(1):12956. doi: 10.1038/s41598-020-69637-0. PMID:32737358[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also
References
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