Title : The structure and mechanism of serine acetyltransferase from Escherichia coli.

Pub. Date : 2004 Sep 24

PMID : 15231846






5 Functional Relationships(s)
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1 On the basis of the geometry around the cysteine binding site, we are able to suggest a mechanism for the O-acetylation of serine by SAT. Serine streptothricin acetyltransferase Escherichia coli
2 Serine acetyltransferase (SAT) catalyzes the first step of cysteine synthesis in microorganisms and higher plants. Cysteine streptothricin acetyltransferase Escherichia coli
3 Here we present the 2.2 A crystal structure of SAT from Escherichia coli, which is a dimer of trimers, in complex with cysteine. Cysteine streptothricin acetyltransferase Escherichia coli
4 This structure shows the mechanism by which cysteine inhibits SAT activity and thus controls its own synthesis. Cysteine streptothricin acetyltransferase Escherichia coli
5 On the basis of the geometry around the cysteine binding site, we are able to suggest a mechanism for the O-acetylation of serine by SAT. Cysteine streptothricin acetyltransferase Escherichia coli