Serine acetyltransferase
From Proteopedia
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| - | <StructureSection load='4n69' size='340' side='right' caption=' | + | <StructureSection load='4n69' size='340' side='right' caption='Serine acetyltransferase complex with serine (PDB code [[4n69]])' scene=''> |
== Function == | == Function == | ||
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== Structural highlights == | == 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. Arg 253 is important for the catalytic efficiency of SAT. Lys230 is required for the cofactor acetyl-CoA binding<ref>PMID:24225955</ref>. | |
</StructureSection> | </StructureSection> | ||
Revision as of 07:49, 21 November 2018
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3D structures of serine acetyltransferase
Updated on 21-November-2018
References
- ↑ Gerlt JA, Babbitt PC, Rayment I. Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity. Arch Biochem Biophys. 2005 Jan 1;433(1):59-70. doi: 10.1016/j.abb.2004.07.034. PMID:15581566 doi:http://dx.doi.org/10.1016/j.abb.2004.07.034
- ↑ Yi H, Dey S, Kumaran S, Lee SG, Krishnan HB, Jez JM. Structure of Soybean Serine Acetyltransferase and Formation of the Cysteine Regulatory Complex as a Molecular Chaperone. J Biol Chem. 2013 Nov 13. PMID:24225955 doi:http://dx.doi.org/10.1074/jbc.M113.527143
