Literature summary for 2.7.13.3 extracted from

Bick, M.J.; Lamour, V.; Rajashankar, K.R.; Gordiyenko, Y.; Robinson, C.V.; Darst, S.A.
How to switch off a histidine kinase: crystal structure of Geobacillus stearothermophilus KinB with the inhibitor Sda (2009), J. Mol. Biol., 386, 163-177.

Search for more literature for 2.7.13.3

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli Rosetta2 DE3 cells	Geobacillus stearothermophilus

Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with inhibitor Sda, crystals only form in the presence of ADP-Mg2+ (but not with ATP or AMPPNP, and not in the absence of nucleotide)	Geobacillus stearothermophilus

Inhibitors

Inhibitors	Comment	Organism	Structure
Sda	potent inhibitor of KinB autophosphorylation, Sda directly inhibits sporulation histidine kinase in response to DNA damage and replication defects, Sda acts to sterically block communication between the catalytic ATP-binding and dimerization/histidinephosphotransfer domains required for autophosphorylation, as well as to sterically block communication between the response regulator Spo0F and DHp domain required for phosphotransfer and phosphatase activities	Geobacillus stearothermophilus

Organism

Organism	UniProt	Comment	Textmining
Geobacillus stearothermophilus	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	autophosphorylation in the presence of ATP	Geobacillus stearothermophilus

Purification (Commentary)

Purification (Comment)	Organism
Ni2+-affinity column chromatography, followed by anion exchange chromatography and gel filtration	Geobacillus stearothermophilus

Subunits

Subunits	Comment	Organism
dimer	x-ray crystallography	Geobacillus stearothermophilus

Synonyms

Synonyms	Comment	Organism
KinB	-	Geobacillus stearothermophilus
sporulation histidine kinase	-	Geobacillus stearothermophilus

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Geobacillus stearothermophilus

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Release 2023.1 (January 2023)