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Literature summary for 7.2.2.14 extracted from

  • Payandeh, J.; Li, C.; Ramjeesingh, M.; Poduch, E.; Bear, C.E.; Pai, E.F.
    Probing structure-function relationships and gating mechanisms in the CorA Mg2+ transport system (2008), J. Biol. Chem., 283, 11721-11733.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21, complementation of Salmonella typhimurium MM281, a strain devoid of all genomic Mg2+ transport systems Thermotoga maritima

Protein Variants

Protein Variants Comment Organism
D253F site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview Thermotoga maritima
D253K site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview Thermotoga maritima
D253W site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview Thermotoga maritima
E206R site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview Thermotoga maritima
E316K site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview Thermotoga maritima
E316K/E320A site-directed mutagenesis, with mutation of Gly4alpha5alpha6, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview Thermotoga maritima
E320K site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview Thermotoga maritima
additional information deletion mutant Gly4alpha5alpha6, site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview Thermotoga maritima
P303I site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview Thermotoga maritima
V194E site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview Thermotoga maritima
V194E/E206R site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview Thermotoga maritima

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Thermotoga maritima 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + Mg2+/out Thermotoga maritima
-
ADP + phosphate + Mg2+/in
-
?

Organism

Organism UniProt Comment Textmining
Thermotoga maritima Q9WZ31 gene corA
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 by nickel affinity chromatography, cleavage of the His-tag, and gel filtration to homogeneity Thermotoga maritima

Renatured (Commentary)

Renatured (Comment) Organism
reconstitution of the purified recombinant enzyme in phosphatidylcholine liposomes, overview Thermotoga maritima

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Mg2+/out
-
Thermotoga maritima ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out CorA contains an unusually long ion pore putatively gated by hydrophobic residues near the intracellular end and by universally conserved asparagine residues at the periplasmic entrance, structure-function relationships and gating mechanisms in the CorA Mg2+ transport system, the intracellular funnel domain constitutes an allosteric regulatory module that can be engineered to promote an activated or closed state, involvement of the alpha5 and alpha6 helices in CorA function, overview Thermotoga maritima ADP + phosphate + Mg2+/in
-
?
additional information CorA is selective for magnesium ions over calcium ions with a 100fold greater uptake rate Thermotoga maritima ?
-
?

Subunits

Subunits Comment Organism
More CorA contains an unusually long ion pore putatively gated by hydrophobic residues near the intracellular end and by universally conserved asparagine residues at the periplasmic entrance Thermotoga maritima

Synonyms

Synonyms Comment Organism
CorA
-
Thermotoga maritima
More the enzyme belongs to the CorA-Alr1-Mrs2 superfamily Thermotoga maritima

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Thermotoga maritima

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
assay at Thermotoga maritima