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Literature summary for 3.6.5.5 extracted from

  • Dick, A.; Graf, L.; Olal, D.; von der Malsburg, A.; Gao, S.; Kochs, G.; Daumke, O.
    Role of nucleotide binding and GTPase domain dimerization in dynamin-like myxovirus resistance protein A for GTPase activation and antiviral activity (2015), J. Biol. Chem., 290, 12779-12792.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.5.5

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of GST- and His-tagged MxA in Escherichia coli strain BL21(DE3) Homo sapiens

Protein Variants

Protein Variants Comment Organism
D250N site-directed mutagenesis, a monomeric mutant, loss of nucleotide binding Homo sapiens
D253N site-directed mutagenesis, a monomeric mutant Homo sapiens
G255E site-directed mutagenesis, a monomeric mutant Homo sapiens
K83A site-directed mutagenesis, the mutant shows reduced dimerization Homo sapiens
M527D site-directed mutagenesis, a monomeric mutant Homo sapiens
M527D/D250N site-directed mutagenesis, a monomeric mutant Homo sapiens
M527D/D250N/D253N site-directed mutagenesis, a monomeric mutant Homo sapiens
M527D/D253N site-directed mutagenesis, a monomeric mutant Homo sapiens
M527D/K83A site-directed mutagenesis, a monomeric mutant Homo sapiens
M527D/T103A site-directed mutagenesis, a monomeric mutant Homo sapiens
additional information analysis of nucleotide binding, dimerization, and GTPase activities of the enzyme mutants, overview Homo sapiens
T103A site-directed mutagenesis, a monomeric mutant Homo sapiens
V268M site-directed mutagenesis, the mutant shows reduced dimerization Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm the enzyme is expressed in the cytoplasm and is partly associated with membranes of the smooth endoplasmic reticulum Homo sapiens 5737
-
endoplasmic reticulum the enzyme is expressed in the cytoplasm and is partly associated with membranes of the smooth endoplasmic reticulum Homo sapiens 5783
-
membrane the enzyme is expressed in the cytoplasm and is partly associated with membranes of the smooth endoplasmic reticulum Homo sapiens 16020
-

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
-
 ?
additional information Homo sapiens MxA recognizes Thogoto virus nucleocapsid proteins independently of nucleotide binding, while both nucleotide binding and hydrolysis are required for the antiviral activity against Thogoto, influenza, and La Crosse viruses. GTP binding facilitates formation of stable MxA assemblies associated with endoplasmic reticulum membranes, whereas nucleotide hydrolysis promotes dynamic redistribution of MxAfrom cellular membranes to viral targets ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P20591
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant GST- and His-tagged MxA from Escherichia coli strain BL21(DE3) by nickel affinity and glutathione affinity chromatography, and gel filtration Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
GTP + H2O = GDP + phosphate analysis of the GTPase mechanism of MxA Homo sapiens
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + H2O
-
 Homo sapiens GDP + phosphate
-
 ?
additional information MxA recognizes Thogoto virus nucleocapsid proteins independently of nucleotide binding, while both nucleotide binding and hydrolysis are required for the antiviral activity against Thogoto, influenza, and La Crosse viruses. GTP binding facilitates formation of stable MxA assemblies associated with endoplasmic reticulum membranes, whereas nucleotide hydrolysis promotes dynamic redistribution of MxAfrom cellular membranes to viral targets Homo sapiens ?
-
 ?
additional information enzyme-nucleotide binding studies, overview Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
More dimerization of MxA via a GTPase domain interface is required for GTP hydrolysis and antiviral activity. Residues in the catalytic center of MxA and the nucleotide itself are essential for G domain dimerization and catalytic activation Homo sapiens

Synonyms

Synonyms Comment Organism
dynamin-like myxovirus resistance protein A
-
 Homo sapiens
Mx GTPase
-
 Homo sapiens
MX1
-
 Homo sapiens
MxA
-
 Homo sapiens
myxovirus resistance 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
7.5
-
 assay at Homo sapiens

General Information

General Information Comment Organism
additional information homology modeling and comparison to human dynamin1 GTPase structure, overview. Most of the residues in the catalytic center are highly conserved between MxA and dynamin, for example the G4 loop mediating specificity for guanine binding Homo sapiens
physiological function myxovirus resistance proteins are key mediators of the interferon-induced innate immune response in vertebrates, role of nucleotide binding and GTPase domain dimerization in dynamin-like myxovirus resistance protein A for GTPase activation and antiviral activity. GTP binding allows GTPase domain dimerization and membrane-associated assembly of MxA, but it is not sufficient to induce a sustained antiviral effect Homo sapiens