Literature summary for 6.1.1.21 extracted from

Qiu, X.; Janson, C.A.; Blackburn, M.N.; Chhohan, I.K.; Hibbs, M.; Abdel-Meguid, S.S.
Cooperative structural dynamics and a novel fidelity mechanism in histidyl-tRNA synthetases (1999), Biochemistry, 38, 12296-12304.

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Cloned(Commentary)

Cloned (Comment)	Organism
overexpression in Escherichia coli DH5alpha	Staphylococcus aureus

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant apoenzyme at 8 mg/ml, sitting drop method, protein solution: 20 mM Tris, pH 7.5, 0.2 M NaCl, 1 mM EDTA, 1 mM DTT, plus equal volume of well solution: 0.1 M sodium citrate, pH 5.6, 0.2 M sodium/potassium tartrate, 1.8 M ammonium sulfate, several days at room temperature, X-ray diffraction structure determination at 2.7 A resolution, and analysis	Staphylococcus aureus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-histidine + tRNAHis	Staphylococcus aureus	-	AMP + diphosphate + L-histidyl-tRNAHis	-	?

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus aureus	P60911	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant from Escherichia coli	Staphylococcus aureus

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis	mechanism, active site structure, ligand induced structural changes, highly cooperative dynamics	Staphylococcus aureus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-histidine + tRNAHis	-	Staphylococcus aureus	AMP + diphosphate + L-histidyl-tRNAHis	-	?
ATP + L-histidine + tRNAHis	histidine A motif, Arg257-Tyr262, is essential for substrate recognition, a loop, Gly52-Lys62, controls the communication between histidine and ATP binding sites, the motif loop, Glu114-Arg120, binds ATP, an insertion domain binds tRNA	Staphylococcus aureus	AMP + diphosphate + L-histidyl-tRNAHis	-	?

Synonyms

Synonyms	Comment	Organism
HisRS	-	Staphylococcus aureus
Histidine translase	-	Staphylococcus aureus
histidine-tRNA ligase	-	Staphylococcus aureus
histidine-tRNA ligase homolog	-	Staphylococcus aureus
Histidyl-transfer ribonucleate synthetase	-	Staphylococcus aureus
Histidyl-tRNA synthetase	-	Staphylococcus aureus
Jo-1	-	Staphylococcus aureus
Jo-1 antigen	-	Staphylococcus aureus
Synthetase, histidyl-transfer ribonucleate	-	Staphylococcus aureus

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Staphylococcus aureus

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Release 2023.1 (January 2023)