Literature summary for 2.5.1.47 extracted from

Dharavath, S.; Raj, I.; Gourinath, S.
Structure-based mutational studies of O-acetylserine sulfhydrylase reveal the reason for the loss of cysteine synthase complex formation in Brucella abortus (2017), Biochem. J., 474, 1221-1239 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Brucella abortus

Crystallization (Commentary)

Crystallization (Comment)	Organism
native enzyme and mutant Q96A/Y125A, to 1.54 and 0.97 A resolution, respectively. OASS does not interact with its cognate serine acetyltransferase C-terminal tail. Crystal structures show that residues Gln96 and Tyr125 occupy the active-site pocket and interfere with the entry of the serine acetyltransferase C-terminal tail	Brucella abortus

Protein Variants

Protein Variants	Comment	Organism
Q96A/Y125A	mutant shows relatively strong binding to serine acetyltransferase C-terminal peptides in comparison with native OASS. The mutant structure looks similar except that the active-site pocket has enough space to bind the serine acetyltransferase C-terminal end	Brucella abortus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Brucella abortus	A0A0F6AQU1	-	-
Brucella abortus S19	A0A0F6AQU1	-	-

Synonyms

Synonyms	Comment	Organism
BAbS19_I09950	-	Brucella abortus
OASS	-	Brucella abortus

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Release 2023.1 (January 2023)