Literature summary for 7.4.2.1 extracted from

Campbell, J.D.; Deol, S.S.; Ashcroft, F.M.; Kerr, I.D.; Sansom, M.S.
Nucleotide-dependent conformational changes in HisP: Molecular dynamics simulations of an ABC transporter nucleotide-binding domain (2004), Biophys. J., 87, 3703-3715.

Search for more literature for 7.4.2.1

Application

Application	Comment	Organism
additional information	conformational changes within HisP that are dependent on the presence of ATP in the binding pocket of the protein, changes are predominantely confined to the alpha-helical subdomain, considerable conformational flexibility in a conserved glutamine-containing loop	Salmonella enterica subsp. enterica serovar Typhimurium

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	conformational changes within HisP are sensitive to the presence/absence of Mg ions bound to the ATP	Salmonella enterica subsp. enterica serovar Typhimurium

Organism

Organism	UniProt	Comment	Textmining
Salmonella enterica subsp. enterica serovar Typhimurium	-	-	-

Synonyms

Synonyms	Comment	Organism
HisP	-	Salmonella enterica subsp. enterica serovar Typhimurium

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)