Literature summary for 3.6.5.5 extracted from

Anand, R.; Eschenburg, S.; Reubold, T.F.
Crystal structure of the GTPase domain and the bundle signalling element of dynamin in the GDP state (2016), Biochem. Biophys. Res. Commun., 469, 76-80 .

Cloned(Commentary)

Cloned (Comment)	Organism
gene DNM1, recombinant expression of the dynamin 1 GTPase domain GG1 from modified pGEX-4T1 vector containing a TEV protease site. The fragments are connected by a linker composed of eight amino acid residues (KHGTDSRV) in Escherichia coli strain BL21 (DE3)	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
GTPase domain and the bundle signalling element of dynamin in the GDP-bound state, GG1, hanging drop vapour diffusion method, mixing of 0.0015 ml of 10 mg/ml GG1 protein solution containing 2 mM GDP and 2 mM MgCl2 with 0.0015 ml of reservoir solution containing 0.1 M Tris, pH 8.0, 26% PEG 3350, and 0.2 M NaSCN, and equilibration against 0.7 ml of reservoir solution, one week, 4°C, X-ray diffraction structure determination and analysis at 1.7-1.8 A resolution, molecular replacement using GG1GDP.AlFx (PDB ID 2X2E) as search model	Homo sapiens

Crystallization (Comment)

Organism

GTPase domain and the bundle signalling element of dynamin in the GDP-bound state, GG1, hanging drop vapour diffusion method, mixing of 0.0015 ml of 10 mg/ml GG1 protein solution containing 2 mM GDP and 2 mM MgCl2 with 0.0015 ml of reservoir solution containing 0.1 M Tris, pH 8.0, 26% PEG 3350, and 0.2 M NaSCN, and equilibration against 0.7 ml of reservoir solution, one week, 4°C, X-ray diffraction structure determination and analysis at 1.7-1.8 A resolution, molecular replacement using GG1GDP.AlFx (PDB ID 2X2E) as search model

Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
GTP + H2O	Homo sapiens	-	GDP + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q05193	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant dynamin 1 GTPase domain GG1 from Escherichia coli strain BL21 (DE3) by glutathione affinity chromatography, tag cleavage by TEV protease, ultrafiltration, and gel filtration	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
GTP + H2O	-	Homo sapiens	GDP + phosphate	-	?
additional information	analysis of the enzyme in GDP-bound state, the switch I region moves away from the active site after GTP hydrolysis and release of inorganic phosphate	Homo sapiens	?	-	-

Subunits

Subunits	Comment	Organism
More	dynamin can be subdivided into five domains: the N-terminal GTPase domain (G domain), the bundle signalling element (BSE), the stalk, the pleckstrin homology domain (PH domain), and the proline-rich domain (PRD). The G domain binds and hydrolyses GTP. The BSE is a three-helix bundle originating from the termini of the G domain and from a more C-terminal helix that fold back towards the N-terminus	Homo sapiens

Synonyms

Synonyms	Comment	Organism
dynamin	-	Homo sapiens
dynamin 1	-	Homo sapiens
GTPase	-	Homo sapiens

General Information

General Information	Comment	Organism
evolution	dynamin is the prototype of a family of large multidomain GTPases. Dynamins and dynamin related proteins constitute a large family of atypical multidomain GTPases that share the common properties of low affinity for guanine nucleotides, high rate of GTP hydrolysis and the ability to oligomerize into helical structures	Homo sapiens
additional information	analysis of the structural changes through the hydrolytic cycle, the GDP state, the GTP state, the transition state, and the nucleotide-free state of dynamin 1, detailed overview. The G domain of dynamin 1 contains five nucleotide binding motifs G1 to G5. G1 comprises the residues 38GGQSAGKS45 and is also known as P-loop or Walker A motif; G2 describes the loop containing the conserved residue T65 and is also called switch I or Walker Bmotif. G3 comprises residues 136DLPG139 and is also called switch II. G4 comprises residues 205TKLD208. G5 comprises residues 236NRSQKDIDGKK246 and is known as the dynamin specific loop (DSL). Interactions of TSL and especially CSL restrict the conformational flexibility of switch II to ensure efficient positioning during catalysis	Homo sapiens
physiological function	dynamin is a key player in clathrin-mediated endocytosis, where it cleaves off vesicles from membranes using the energy from GTP hydrolysis	Homo sapiens