1t3d
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(New page: 200px<br /><applet load="1t3d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t3d, resolution 2.20Å" /> '''Crystal structure of...)
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Revision as of 00:50, 21 November 2007
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Crystal structure of Serine Acetyltransferase from E.coli at 2.2A
Overview
Serine acetyltransferase (SAT) catalyzes the first step of cysteine, synthesis in microorganisms and higher plants. Here we present the 2.2 A, crystal structure of SAT from Escherichia coli, which is a dimer of, trimers, in complex with cysteine. The SAT monomer consists of an, amino-terminal alpha-helical domain and a carboxyl-terminal left-handed, beta-helix. We identify His(158) and Asp(143) as essential residues that, form a catalytic triad with the substrate for acetyl transfer. This, structure shows the mechanism by which cysteine inhibits SAT activity and, thus controls its own synthesis. Cysteine is found to bind at the serine, substrate site and not the acetyl-CoA site that had been reported, previously. 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., We also compare the structure of SAT with other left-handed beta-helical, structures.
About this Structure
1T3D is a Single protein structure of sequence from Escherichia coli with CYS as ligand. Active as Serine O-acetyltransferase, with EC number 2.3.1.30 Full crystallographic information is available from OCA.
Reference
The structure and mechanism of serine acetyltransferase from Escherichia coli., Pye VE, Tingey AP, Robson RL, Moody PC, J Biol Chem. 2004 Sep 24;279(39):40729-36. Epub 2004 Jul 1. PMID:15231846
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