Literature summary for 3.6.5.5 extracted from

Srinivasan, S.; Dharmarajan, V.; Reed, D.K.; Griffin, P.R.; Schmid, S.L.
Identification and function of conformational dynamics in the multidomain GTPase dynamin (2016), EMBO J., 35, 443-457 .

Search for more literature for 3.6.5.5

Activating Compound

Activating Compound	Comment	Organism	Structure
liposome	liposome-stimulated GTPase activity of Dyn1	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	engineering of dynamin constructs locked in either the closed or open state by chemical cross-linking or deletion mutagenesis. Design of dynamin mutants to restrict the PHD in the closed (Dyn1Closed) or open (Dyn1DELTADELTA) state. The stimulation of GTPase activity of Dyn1DELTADELTA mutant by liposomes is reduced compared to the wild-type enzyme. Ability of wild-type Dyn1, and mutant Dyn1CC and Dyn1Closed to catalyze membrane fission and vesicle release from SUPER templates, overview	Homo sapiens
S619L	site-directed mutagenesis, the pleckstrin homology domain (PHD) conformational switch is impaired by the centronuclear myopathy-causing disease mutation. The temperature-sensitive phenotype of the Dyn1S619L mutant reflects temperature-sensitive changes in the steady-state conformation(s) adopted by the PHD	Homo sapiens
Y354C	site-directed mutagenesis, interaction analysis with Dyn2L354C-IAEDANS mutant, membrane binding and consequent opening of PHD in mutants Dyn1Y354C-IAEDANS and Dyn2L354C-IAEDANS, overview	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytosol	-	Homo sapiens	5829	-
membrane	-	Homo sapiens	16020	-
additional information	the enzyme domain PHD orientation serves as a conformation switch between cytosolic and membrane-bound states	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	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
GTP + H2O	-	Homo sapiens	GDP + phosphate	-	?
additional information	behaviour analysis of the enzyme in nucleotide and/or membrane binding, detailed overview. Nucleotide-dependent changes in PHD-membrane interactions and the non-hydrolyzable GTP analogue, GMPPCP (beta-gamma-methyleneguanosine 5'-triphosphate)-dependent loosening of the scaffold. Ability of wild-type Dyn1, and mutant Dyn1CC and Dyn1Closed to catalyze membrane fission and vesicle release from SUPER templates, overview	Homo sapiens	?	-	-

Subunits

Subunits	Comment	Organism
More	enzyme domain structure, overview. Hydrogen-deuterium exchange kinetics reveal long-range nucleotide- and/or membrane-binding-driven conformational changes in dynamin	Homo sapiens

Synonyms

Synonyms	Comment	Organism
Dyn1	-	Homo sapiens
dynamin	-	Homo sapiens
dynamin1	-	Homo sapiens
multidomain GTPase	-	Homo sapiens

General Information

General Information	Comment	Organism
malfunction	the pleckstrin homology domain (PHD) conformational switch is impaired by a centronuclear myopathy-causing disease mutation, S619L, highlighting the physiological significance of its role in regulating dynamin function	Homo sapiens
additional information	the BSE and PHD are mobile elements necessary for dynamin function. Hydrogen-deuterium exchange coupled with mass spectrometry revealed global nucleotide- and membrane-binding-dependent conformational changes, as well as the existence of an allosteric relay element in the a2S helix of the dynamin stalk domain. FRET analyses detect large movements of the pleckstrin homology domain (PHD) from a closed conformation docked near the stalk to an open conformation able to interact with membranes. PHD movements function as a conformational switch to regulate dynamin self-assembly, membrane binding, and fission. The wild-type isozyme Dyn2 exhibits greater curvature dependence for membrane binding than wild-type isozyme Dyn1	Homo sapiens
physiological function	coordinated conformational changes regulate dynamin function and couple membrane binding, oligomerization, and GTPase activity during dynamin-catalyzed membrane fission	Homo sapiens

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Release 2023.1 (January 2023)