5owv
From Proteopedia
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==An oligomerised bacterial dynamin pair provides a mechanism for the long-range sensing and tethering of membranes== | ==An oligomerised bacterial dynamin pair provides a mechanism for the long-range sensing and tethering of membranes== | ||
| - | <StructureSection load='5owv' size='340' side='right' caption='[[5owv]], [[Resolution|resolution]] 3.72Å' scene=''> | + | <StructureSection load='5owv' size='340' side='right'caption='[[5owv]], [[Resolution|resolution]] 3.72Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5owv]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OWV OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5owv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OWV FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.72Å</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=5owv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5owv OCA], [https://pdbe.org/5owv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5owv RCSB], [https://www.ebi.ac.uk/pdbsum/5owv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5owv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DLP1_CAMJJ DLP1_CAMJJ] The heterotetrameric DLP1(2)-DLP2(2) complex tethers liposomes and may mediate their fusion. Initial binding is probably mediated by DLP1, while DLP2 couples DLP1 subunits and increases the effective reach of the complex up to 45 nm. The role of the nucleotide is unknown. This subunit alone weakly binds to liposomes; GTP, GDP, GMPPCP and GMPPNP do not change heterotetramer binding. Tetramerization is required for GTPase activity, suggesting the GTPase domains (dynamin-type G) from DLP1 and DLP2 must dimerize to reconstitute the GTPase active site.<ref>PMID:30131557</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5owv" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5owv" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Campylobacter jejuni]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Liu JW]] |
| - | [[Category: | + | [[Category: Low HH]] |
| - | [[Category: | + | [[Category: Noel JK]] |
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Current revision
An oligomerised bacterial dynamin pair provides a mechanism for the long-range sensing and tethering of membranes
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