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Literature summary for 3.6.5.5 extracted from

  • Wenger, J.; Klinglmayr, E.; Froehlich, C.; Eibl, C.; Gimeno, A.; Hessenberger, M.; Puehringer, S.; Daumke, O.; Goettig, P.
    Functional mapping of human dynamin-1-like GTPase domain based on x-ray structure analyses (2013), PLoS ONE, 8, e71835.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of C-terminally His6-tagged wild-type and mutants of DNM1L isoform 2 Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
purified wild-type and mutants of DNM1L isoform 2, mixing of 0.001 ml of 1.2 mg/ml protein with 0.001 ml of reservoir solution containing 0.1 M sodium citrate pH 5, 27.5% PEG 3000, equilibration against 0.4 ml of reservoir solution, 3-5 days, for co-crystallization of the enzyme with a non-hydrolyzable GTP analogue the protein is incubated with 1 mM GMP-PNP and 4 mM MgCl2, and then purified by gel filtration, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement using human dynamin-1 structure, PDB ID 3SNH Homo sapiens

Protein Variants

Protein Variants Comment Organism
D146A site-directed mutagenesis Homo sapiens
D190A site-directed mutagenesis Homo sapiens
D218A site-directed mutagenesis Homo sapiens
E81A site-directed mutagenesis Homo sapiens
E81A/E82A site-directed mutagenesis Homo sapiens
G149A site-directed mutagenesis Homo sapiens
K216A site-directed mutagenesis Homo sapiens
K38A site-directed mutagenesis Homo sapiens
N246A site-directed mutagenesis Homo sapiens
Q34A site-directed mutagenesis Homo sapiens
S35A site-directed mutagenesis Homo sapiens
S39A site-directed mutagenesis Homo sapiens
S40A site-directed mutagenesis Homo sapiens
T59A site-directed mutagenesis Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required for activity 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 O00429
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
DNM1L
-
Homo sapiens
dynamin-1-like GTPase
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 7.4 assay at Homo sapiens

General Information

General Information Comment Organism
evolution the enzyme is a member of the dynamin superfamily that comprises a family of conserved GTPases. Most dynamin superfamily members contain five conserved GTP-binding motifs (G1-5), similar to small Ras-like GTPases Homo sapiens
malfunction mutated Glu81 and Glu82 in the unique 16-residue insertion of the enzyme influence the activity significantly. Mutations of Gln34, Ser35, and Asp190 in the predicted assembly interface interfer with dimerization of the GTPase domain induced by a transition state analogue and lead to a loss of the lipid-stimulated GTPase activity Homo sapiens
additional information the GTPase domain of the enzyme is structurally related to that of dynamin and binds the nucleotide 5'-guanylyl-imidodiphosphate (GMP-PNP) via five highly conserved motifs, whereas the BSE folds into a pocket at the opposite side. Residues essential for the GTPase reaction are Lys38, Ser39 and Ser40 in the phosphate binding loop, Thr59 from switch I, Asp146 and Gly149 from switch II, Lys216 and Asp218 in the G4 element, as well as Asn246 in the G5 element. Conformational changes upon GTP-binding in the active site, and overall structure of the DNM1L GTPase-GED fusion protein, overview Homo sapiens
physiological function human dynamin-1-like protein is a GTP-driven molecular machine that segregates mitochondria and peroxisomes, catalytic mechanism involving dimerization of their GTPase domains, overview Homo sapiens