Literature summary for 2.7.13.3 extracted from

Monk, I.; Shaikh, N.; Begg, S.; Gajdiss, M.; Sharkey, L.; Lee, J.; Pidot, S.; Seemann, T.; Kuiper, M.; Winnen, B.; Hvorup, R.; Collins, B.; Bierbaum, G.; Udagedara, S.; Morey, J.; Pulyani, N.; Howden, B.; Maher, M.; McDevitt, C.; King, G.; Stinear, T.
Zinc-binding to the cytoplasmic PAS domain regulates the essential WalK histidine kinase of Staphylococcus aureus (2019), Nat. Commun., 10, 3067 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of the cytoplasmic PAS domain, residues valine 251 to arginine 376. The metal-binding site comprises a single Zn2+ ion bound by the atoms Ndelta1 from His271, Odelta1 from Asp274, Ndelta1 from His364 and Oepsilon2 from Glu368 in a slightly distorted tetrahedral coordination geometry	Staphylococcus aureus

Protein Variants

Protein Variants	Comment	Organism
H271Y	introducing the mutation into wild-type activates the WalKR regulon. Zn2+ is tetrahedrally-coordinated by four amino acids including H271. The H271Y mutation abrogates metal binding, increasing WalK kinase activity and WalR phosphorylation. The mutant strain shows increased lysostaphin and vancomycin sensitivity	Staphylococcus aureus

Inhibitors

Inhibitors	Comment	Organism	Structure
Zn2+	Zn2+ binding negatively regulates the WalKR regulon. Zn2+ binding directly influences the relative positioning of the PAS and catalytic domains of WalK	Staphylococcus aureus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus aureus	Q9RDT3	-	-

Synonyms

Synonyms	Comment	Organism
WalK	-	Staphylococcus aureus
YycFG	-	Staphylococcus aureus

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Release 2023.1 (January 2023)