Literature summary for 7.5.2.1 extracted from

Hsu, W.L.; Furuta, T.; Sakurai, M.
The mechanism of nucleotide-binding domain dimerization in the intact maltose transporter as studied by all-atom molecular dynamics simulations (2018), Proteins, 86, 237-247 .

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required in form of Mg2+-ATP	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O + maltose-[maltose-binding protein][side 1]	Escherichia coli	-	ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P68187 and P68183 and P02916 and P0AEX9	subunits MalK, MalG, MalF, and MalE	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O + maltose-[maltose-binding protein][side 1]	-	Escherichia coli	ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]	-	?

Synonyms

Synonyms	Comment	Organism
MalFGK2-E	the maltose transporter has 4 major domains: the heterodimeric transmembrane domains MalF and MalG, and the homodimeric nucleotide-binding domains MalK2	Escherichia coli
maltose transporter	-	Escherichia coli

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Release 2023.1 (January 2023)