6fgz: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 6fgz is ~~ON HOLD~~

==Cyanidioschyzon merolae Dnm1 (CmDnm1)==

== 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>

== 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.

~~Authors~~:

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>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased Structures~~]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Bohuszewicz, O]]

[[Category: Low, H H]]

[[Category: Dynamin]]

[[Category: Lipid binding protein]]

[[Category: Mitochondrial fission]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6fgz is ON HOLD
+==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>
+<div style="background-color:#fffaf0;">
+== 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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6fgz" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Bohuszewicz, O]]
+[[Category: Low, H H]]
+[[Category: Dynamin]]
+[[Category: Lipid binding protein]]
+[[Category: Mitochondrial fission]]