Literature summary for 7.6.2.8 extracted from

Kandt, C.; Tieleman, D.P.
Holo-BtuF stabilizes the open conformation of the vitamin B12 ABC transporter BtuCD (2010), Proteins, 78, 738-753.

Search for more literature for 7.6.2.8

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Escherichia coli	BtuCD forms a stable complex with the vitamin B12 binding protein BtuF. Using protein docking and MD simulation studies it is shown that holo-BtuF stabilizes the open conformation of BtuCD, whereas the transporter begins to close again when BtuF or vitamin B12 is removed suggesting BtuCD-F is capable of substrate sensitivity. BtuC transmembrane helices 3 and 5, the L-loops and the adjacent helices comprised of BtuC residues 170-180 are identified as hotspots of conformational change	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	BtuCD forms a stable complex with the vitamin B12 binding protein BtuF. Using protein docking and MD simulation studies it is shown that holo-BtuF stabilizes the open conformation of BtuCD, whereas the transporter begins to close again when BtuF or vitamin B12 is removed suggesting BtuCD-F is capable of substrate sensitivity. BtuC transmembrane helices 3 and 5, the L-loops and the adjacent helices comprised of BtuC residues 170-180 are identified as hotspots of conformational change	Escherichia coli	?	-	?

Synonyms

Synonyms	Comment	Organism
BtuCD	-	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)