View source for 9em9


==Structure of SynDLP MGD with GMPPNP==
<StructureSection load='9em9' size='340' side='right'caption='[[9em9]], [[Resolution|resolution]] 3.76&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9em9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9EM9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9EM9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.76&#8491;</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=9em9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9em9 OCA], [https://pdbe.org/9em9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9em9 RCSB], [https://www.ebi.ac.uk/pdbsum/9em9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9em9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/P73765_SYNY3 P73765_SYNY3] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
SynDLP, a dynamin-like protein (DLP) encoded in the cyanobacterium Synechocystis sp. PCC 6803, has recently been identified to be structurally highly similar to eukaryotic dynamins. To elucidate structural changes during guanosine triphosphate (GTP) hydrolysis, we solved the cryoelectron microscopy (cryo-EM) structures of oligomeric full-length SynDLP after addition of guanosine diphosphate (GDP) at 4.1 A and GTP at 3.6-A resolution as well as a GMPPNP-bound dimer structure of a minimal G-domain construct of SynDLP at 3.8-A resolution. In comparison with what has been seen in the previously resolved apo structure, we found that the G-domain is tilted upward relative to the stalk upon GTP hydrolysis and that the G-domain dimerizes via an additional extended dimerization domain not present in canonical G-domains. When incubated with lipid vesicles, we observed formation of irregular tubular SynDLP assemblies that interact with negatively charged lipids. Here, we provide the structural framework of a series of different functional SynDLP assembly states during GTP turnover.

Structural basis for GTPase activity and conformational changes of the bacterial dynamin-like protein SynDLP.,Junglas B, Gewehr L, Mernberger L, Schonnenbeck P, Jilly R, Hellmann N, Schneider D, Sachse C Cell Rep. 2024 Aug 27;43(9):114657. doi: 10.1016/j.celrep.2024.114657. PMID:39207903<ref>PMID:39207903</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9em9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synechocystis sp. PCC 6803]]
[[Category: Gewehr L]]
[[Category: Junglas B]]
[[Category: Sachse C]]
[[Category: Schneider D]]
[[Category: Schoennenbeck P]]