Serine acetyltransferase

spinqualitylabelsall models Serine acetyltransferase complex with serine and phosphate (PDB code 4n69) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Serine acetyltransferase (SAT) catalyzes the reaction converting serine to O-acetyl-serine using acetyl-CoA as a cofactor. This reaction is the first step in the synthesis of cysteine in bacteria and plants. SAT is regulated by a feedback inhibition by ots end product - cysteine. Structural highlights The structure of the complex of SAT with its substrate serine suggest that His169 and Asp154 form a catalytic dyad and that His189 may stabilize the oxyanion intermediate. Glu177 helps to position Arg203 and His204 for serine binding (water molecules are shown as red spheres). Arg253 is important for the catalytic efficiency of SAT. Lys230 is required for the cofactor acetyl-CoA binding.

3D structures of serine acetyltransferase

Updated on 15-November-2023

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• Serine acetyltransferase
  • 4n6a – sSAT – soybean
    
  • 1ssm, 1s80 – HiSAT – Haemophilus influenzae
    
  • 3p1b – EhSAT – Entamoeba histolyca
    
  • 4hzc – BaSAT – Brucella abortus
    
  • 3f1x – SAT – Bacterioides vulgatus
    
  • 6lcn – SAT – Planctopirus limnophila<br />
• Serine acetyltransferase complex with amino acid
  • 4n69 – sSAT + Ser
    
  • 1ssq – HiSAT + Cys
    
  • 1t3d – SAT + Cys – Escherichia coli
    
  • 3gvd – SAT + Cys – Yersinia pestis
    
  • 3p47, 7bw9 – EhSAT + Cys
    
  • 3q1x – EhSAT + Ser
    
  • 4h7o – SAT + Cys + Arg – Vibrio cholerae
    
  • 6jvu – SAT + Cys – Klebsiella pneumoniae
    
  • 7ra4 – NgSAT + Ser – Neisseria gonorrhoeae
    
  • 6wye – NgSAT + malate
    
  • 7e3y – SAT + Cys – Salmonella typhimurium
    
• Serine acetyltransferase complex with acetyl-CoA
  • 4n6b – sSAT + Acetyl CoA
    
  • 1sst – HiSAT + Acetyl CoA
    
  • 4hzd – BaSAT + Acetyl CoA
    

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