Galactoside O-acetyltransferase

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The structure of the complex of GAT with <scene name='80/801781/Cv/3'>the cofactor acetyl-CoA shows that the latter binds to residues in a crevice between two subunits</scene><ref name="GAT"/>. Water molecule shown as red sphere.
The structure of the complex of GAT with <scene name='80/801781/Cv/3'>the cofactor acetyl-CoA shows that the latter binds to residues in a crevice between two subunits</scene><ref name="GAT"/>. Water molecule shown as red sphere.
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*<scene name='80/801781/Cv/5'>Acetyl-CoA is in a crevice between two subunits</scene>.
</StructureSection>
</StructureSection>

Current revision

Galactoside O-acetyltransferase complex with acetyl-CoA (PDB code 1krr)

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3D structures of galactoside O-acetyltransferase

Updated on 10-December-2018

1kqa, 1krr – EcGAT + Acetyl CoA – Escherichia coli
1kru, 1krv – EcGAT + Acetyl CoA + galactopyranose derivative
3ftt – SaGAT – Staphylococcus aureus
3v4e, 5u2k, 5v0z – SaGAT + Acetyl CoA
3vbi – BcGAT + Acetyl CoA + TDP derivative – Bacillus cereus
3vbn, 3vbp, 3vbk, 3vbl, 3vbm – BcGAT (mutant) + Acetyl CoA + TDP derivative
3vbj – BcGAT + butyryl CoA + TDP

References

  1. 1.0 1.1 Wang XG, Olsen LR, Roderick SL. Structure of the lac operon galactoside acetyltransferase. Structure. 2002 Apr;10(4):581-8. PMID:11937062
  2. Roderick SL. The lac operon galactoside acetyltransferase. C R Biol. 2005 Jun;328(6):568-75. doi: 10.1016/j.crvi.2005.03.005. PMID:15950163 doi:http://dx.doi.org/10.1016/j.crvi.2005.03.005

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Alexander Berchansky, Michal Harel

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