View source for 6fgz


==Cyanidioschyzon merolae Dnm1 (CmDnm1)==
<StructureSection load='6fgz' size='340' side='right' caption='[[6fgz]], [[Resolution|resolution]] 7.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6fgz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FGZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FGZ FirstGlance]. <br>
</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=6fgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fgz OCA], [http://pdbe.org/6fgz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fgz RCSB], [http://www.ebi.ac.uk/pdbsum/6fgz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fgz ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Dynamin 1-like proteins (DNM1-L) are mechanochemical GTPases that induce membrane fission in mitochondria and peroxisomes. Their mechanism depends on conformational changes driven by nucleotide and lipid cycling. Here we show the crystal structure of a mitochondrial fission dynamin (CmDnm1) from the algae Cyanidioschyzon merolae. Unlike other eukaryotic dynamin structures, CmDnm1 is in a hinge 1 closed conformation, with the GTPase domain compacted against the stalk. Within the crystal, CmDnm1 packs as a diamond-shaped tetramer that is consistent with an inactive off-membrane state. Crosslinking, photoinduced electron transfer assays, and electron microscopy verify these structures. In vitro, CmDnm1 forms concentration-dependent rings and protein-lipid tubes reminiscent of DNM1-L and classical dynamin with hinge 1 open. Our data provides a mechanism for filament collapse and membrane release that may extend to other dynamin family members. Additionally, hinge 1 closing may represent a key conformational change that contributes to membrane fission.

Structure of a mitochondrial fission dynamin in the closed conformation.,Bohuszewicz O, Low HH Nat Struct Mol Biol. 2018 Aug;25(8):722-731. doi: 10.1038/s41594-018-0097-6. Epub, 2018 Jul 30. PMID:30061604<ref>PMID:30061604</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6fgz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bohuszewicz, O]]
[[Category: Low, H H]]
[[Category: Dynamin]]
[[Category: Lipid binding protein]]
[[Category: Mitochondrial fission]]