6jsj
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structural analysis of a trimeric assembly of the mitochondrial dynamin-like GTPase Mgm1== | |
| + | <StructureSection load='6jsj' size='340' side='right'caption='[[6jsj]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6jsj]] is a 3 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=6JSJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JSJ 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]] 3.2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</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=6jsj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jsj OCA], [https://pdbe.org/6jsj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jsj RCSB], [https://www.ebi.ac.uk/pdbsum/6jsj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jsj ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MGM1_YEAST MGM1_YEAST] Dynamin-related GTPase required for mitochondrial fusion. Coordinates interaction between the inner and outer mitochondrial membrane to promote the formation of the double membrane.<ref>PMID:10037792</ref> <ref>PMID:12566426</ref> <ref>PMID:12707284</ref> <ref>PMID:15087460</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The fusion of inner mitochondrial membranes requires dynamin-like GTPases, Mgm1 in yeast and OPA1 in mammals, but how they mediate membrane fusion is poorly understood. Here, we determined the crystal structure of Saccharomyces cerevisiae short Mgm1 (s-Mgm1) in complex with GDP. It revealed an N-terminal GTPase (G) domain followed by two helix bundles (HB1 and HB2) and a unique C-terminal lipid-interacting stalk (LIS). Dimers can form through antiparallel HB interactions. Head-to-tail trimers are built by intermolecular interactions between the G domain and HB2-LIS. Biochemical and in vivo analyses support the idea that the assembly interfaces observed here are native and critical for Mgm1 function. We also found that s-Mgm1 interacts with negatively charged lipids via both the G domain and LIS. Based on these observations, we propose that membrane targeting via the G domain and LIS facilitates the in cis assembly of Mgm1, potentially generating a highly curved membrane tip to allow inner membrane fusion. | ||
| - | + | Structural analysis of a trimeric assembly of the mitochondrial dynamin-like GTPase Mgm1.,Yan L, Qi Y, Ricketson D, Li L, Subramanian K, Zhao J, Yu C, Wu L, Sarsam R, Wong M, Lou Z, Rao Z, Nunnari J, Hu J Proc Natl Acad Sci U S A. 2020 Feb 10. pii: 1919116117. doi:, 10.1073/pnas.1919116117. PMID:32041880<ref>PMID:32041880</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Li | + | <div class="pdbe-citations 6jsj" style="background-color:#fffaf0;"></div> |
| - | [[Category: Yan | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae S288C]] | ||
| + | [[Category: Li L]] | ||
| + | [[Category: Yan L]] | ||
Current revision
Structural analysis of a trimeric assembly of the mitochondrial dynamin-like GTPase Mgm1
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