5d3q: Difference between revisions
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==Dynamin 1 GTPase-BSE fusion dimer complexed with GDP== | |||
<StructureSection load='5d3q' size='340' side='right'caption='[[5d3q]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5d3q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D3Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D3Q 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]] 1.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</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=5d3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d3q OCA], [https://pdbe.org/5d3q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d3q RCSB], [https://www.ebi.ac.uk/pdbsum/5d3q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d3q ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/DYN1_HUMAN DYN1_HUMAN] Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. Involved in receptor-mediated endocytosis. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Dynamin is the prototype of a family of large multi-domain GTPases. The 100 kDa protein is a key player in clathrin-mediated endocytosis, where it cleaves off vesicles from membranes using the energy from GTP hydrolysis. We have solved the high resolution crystal structure of a fusion protein of the GTPase domain and the bundle signalling element (BSE) of dynamin 1 liganded with GDP. The structure provides a hitherto missing snapshot of the GDP state of the hydrolytic cycle of dynamin and reveals how the switch I region moves away from the active site after GTP hydrolysis and release of inorganic phosphate. Comparing our structure of the GDP state with the known structures of the GTP state, the transition state and the nucleotide-free state of dynamin 1 we describe the structural changes through the hydrolytic cycle. | |||
Crystal structure of the GTPase domain and the bundle signalling element of dynamin in the GDP state.,Anand R, Eschenburg S, Reubold TF Biochem Biophys Res Commun. 2016 Jan 1;469(1):76-80. doi:, 10.1016/j.bbrc.2015.11.074. Epub 2015 Nov 21. PMID:26612256<ref>PMID:26612256</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Anand | <div class="pdbe-citations 5d3q" style="background-color:#fffaf0;"></div> | ||
[[Category: Eschenburg | |||
[[Category: Reubold | ==See Also== | ||
*[[Dynamin|Dynamin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Anand R]] | |||
[[Category: Eschenburg S]] | |||
[[Category: Reubold TF]] | |||
Latest revision as of 14:24, 10 January 2024
Dynamin 1 GTPase-BSE fusion dimer complexed with GDPDynamin 1 GTPase-BSE fusion dimer complexed with GDP
Structural highlights
FunctionDYN1_HUMAN Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. Involved in receptor-mediated endocytosis. Publication Abstract from PubMedDynamin is the prototype of a family of large multi-domain GTPases. The 100 kDa protein is a key player in clathrin-mediated endocytosis, where it cleaves off vesicles from membranes using the energy from GTP hydrolysis. We have solved the high resolution crystal structure of a fusion protein of the GTPase domain and the bundle signalling element (BSE) of dynamin 1 liganded with GDP. The structure provides a hitherto missing snapshot of the GDP state of the hydrolytic cycle of dynamin and reveals how the switch I region moves away from the active site after GTP hydrolysis and release of inorganic phosphate. Comparing our structure of the GDP state with the known structures of the GTP state, the transition state and the nucleotide-free state of dynamin 1 we describe the structural changes through the hydrolytic cycle. Crystal structure of the GTPase domain and the bundle signalling element of dynamin in the GDP state.,Anand R, Eschenburg S, Reubold TF Biochem Biophys Res Commun. 2016 Jan 1;469(1):76-80. doi:, 10.1016/j.bbrc.2015.11.074. Epub 2015 Nov 21. PMID:26612256[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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