Crystal structure of the GTPase domain and the bundle signalling element of dynamin in the GDP state
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...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2016-01, Vol.469 (1), p.76-80 |
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| creator | Anand, Roopsee Eschenburg, Susanne Reubold, Thomas F. |
| description | 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.
•High resolution crystal structure of the GDP-state of a dynamin 1 GTPase-BSE fusion.•Visualizes one of the key states of the hydrolytic cycle of dynamin.•The dynamin-specific loop forms a helix as soon as a guanine base is present. |
| doi_str_mv | 10.1016/j.bbrc.2015.11.074 |
| format | Article |
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•High resolution crystal structure of the GDP-state of a dynamin 1 GTPase-BSE fusion.•Visualizes one of the key states of the hydrolytic cycle of dynamin.•The dynamin-specific loop forms a helix as soon as a guanine base is present.</description><subject>60 APPLIED LIFE SCIENCES</subject><subject>active sites</subject><subject>Binding Sites</subject><subject>bovine spongiform encephalopathy</subject><subject>CRYSTAL STRUCTURE</subject><subject>Crystallography</subject><subject>CRYSTALS</subject><subject>Dynamin</subject><subject>dynamins</subject><subject>Dynamins - chemistry</subject><subject>Dynamins - ultrastructure</subject><subject>Endocytosis</subject><subject>energy</subject><subject>Enzyme Activation</subject><subject>GTP Phosphohydrolases - chemistry</subject><subject>GTP Phosphohydrolases - ultrastructure</subject><subject>GTPase</subject><subject>GUANINE</subject><subject>Guanosine Diphosphate - chemistry</subject><subject>guanosine triphosphate</subject><subject>HYDROLYSIS</subject><subject>Hydrolytic cycle</subject><subject>LIGANDS</subject><subject>MEMBRANES</subject><subject>Molecular Docking Simulation</subject><subject>NUCLEOTIDES</subject><subject>PHOSPHATES</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein Structure, Tertiary</subject><subject>PROTEINS</subject><subject>X RADIATION</subject><subject>X-ray structure</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUGL1TAUhYMoznP0D7jQghs3rblpmzbgZnjqKAw44Ay4C2ly8yaPNh2TVHj_3nQ6upQEApfvHHLuIeQ10Aoo8A_HahiCrhiFtgKoaNc8ITuggpYMaPOU7CilvGQCfp6RFzEeKQVouHhOzhjnwFjLd8TswykmNRYxhUWnJWAx2yLdYXF5c60iFmaelPOF8uZhOizejFhEd_BqHJ0_FDjihD6tMnPyaspwvg8On66zrUr4kjyzaoz46vE9J7dfPt_sv5ZX3y-_7S-uSt3QPpUGOuwZYMdU17ZqwJrWjTCcWotDoxVltgXGLRuavu8GkQ8FavOgFyYD9Tl5t_nOMTkZtUuo7_TsPeokc17RQMsz9X6j7sP8a8GY5OSixnFUHuclSuhaVre1EJBRtqE6zDEGtPI-uEmFkwQq1w7kUa4dyLUDCSBzB1n05tF_GSY0_yR_l56Btxtg1SzVIbgob39kB54LEiuUiY8bgXlbvx2GNQx6jcaFNYuZ3f9-8AeNmKAZ</recordid><startdate>20160101</startdate><enddate>20160101</enddate><creator>Anand, Roopsee</creator><creator>Eschenburg, Susanne</creator><creator>Reubold, Thomas F.</creator><general>Elsevier Inc</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>20160101</creationdate><title>Crystal structure of the GTPase domain and the bundle signalling element of dynamin in the GDP state</title><author>Anand, Roopsee ; Eschenburg, Susanne ; Reubold, Thomas F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c408t-d17e821e72a755abe30349d60ffeb4ca02f5126f2b4887b9b9b010f6f289db4c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>active sites</topic><topic>Binding Sites</topic><topic>bovine spongiform encephalopathy</topic><topic>CRYSTAL STRUCTURE</topic><topic>Crystallography</topic><topic>CRYSTALS</topic><topic>Dynamin</topic><topic>dynamins</topic><topic>Dynamins - chemistry</topic><topic>Dynamins - ultrastructure</topic><topic>Endocytosis</topic><topic>energy</topic><topic>Enzyme Activation</topic><topic>GTP Phosphohydrolases - chemistry</topic><topic>GTP Phosphohydrolases - ultrastructure</topic><topic>GTPase</topic><topic>GUANINE</topic><topic>Guanosine Diphosphate - chemistry</topic><topic>guanosine triphosphate</topic><topic>HYDROLYSIS</topic><topic>Hydrolytic cycle</topic><topic>LIGANDS</topic><topic>MEMBRANES</topic><topic>Molecular Docking Simulation</topic><topic>NUCLEOTIDES</topic><topic>PHOSPHATES</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Protein Structure, Tertiary</topic><topic>PROTEINS</topic><topic>X RADIATION</topic><topic>X-ray structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Anand, Roopsee</creatorcontrib><creatorcontrib>Eschenburg, Susanne</creatorcontrib><creatorcontrib>Reubold, Thomas F.</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Anand, Roopsee</au><au>Eschenburg, Susanne</au><au>Reubold, Thomas F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structure of the GTPase domain and the bundle signalling element of dynamin in the GDP state</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2016-01-01</date><risdate>2016</risdate><volume>469</volume><issue>1</issue><spage>76</spage><epage>80</epage><pages>76-80</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>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.
•High resolution crystal structure of the GDP-state of a dynamin 1 GTPase-BSE fusion.•Visualizes one of the key states of the hydrolytic cycle of dynamin.•The dynamin-specific loop forms a helix as soon as a guanine base is present.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>26612256</pmid><doi>10.1016/j.bbrc.2015.11.074</doi><tpages>5</tpages></addata></record> |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | 60 APPLIED LIFE SCIENCES active sites Binding Sites bovine spongiform encephalopathy CRYSTAL STRUCTURE Crystallography CRYSTALS Dynamin dynamins Dynamins - chemistry Dynamins - ultrastructure Endocytosis energy Enzyme Activation GTP Phosphohydrolases - chemistry GTP Phosphohydrolases - ultrastructure GTPase GUANINE Guanosine Diphosphate - chemistry guanosine triphosphate HYDROLYSIS Hydrolytic cycle LIGANDS MEMBRANES Molecular Docking Simulation NUCLEOTIDES PHOSPHATES Protein Binding Protein Conformation Protein Structure, Tertiary PROTEINS X RADIATION X-ray structure |
| title | Crystal structure of the GTPase domain and the bundle signalling element of dynamin in the GDP state |
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