1krv
Galactoside Acetyltransferase in Complex with CoA and PNP-beta-GalGalactoside Acetyltransferase in Complex with CoA and PNP-beta-Gal
Structural highlights
Function[THGA_ECOLI] May assist cellular detoxification by acetylating non-metabolizable pyranosides, thereby preventing their reentry into the cell. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe galactoside acetyltransferase (thiogalactoside transacetylase) of Escherichia coli (GAT, LacA, EC 2.3.1.18) is a gene product of the classical lac operon. GAT may assist cellular detoxification by acetylating nonmetabolizable pyranosides, thereby preventing their reentry into the cell. The structure of GAT has been solved in binary complexes with acetyl-CoA or CoA and in ternary complexes with CoA and the nonphysiological acceptor substrates isopropyl beta-D-thiogalactoside (IPTG) or p-nitrophenyl beta-D-galactopyranoside (PNPbetaGal). A hydrophobic cleft that binds the thioisopropyl and p-nitrophenyl aglycones of IPTG and PNPbetaGal may discriminate against substrates with hydrophilic substituents at this position, such as lactose, or inducers of the lac operon. An extended loop projecting from the left-handed parallel beta helix domain contributes His115, which is in position to facilitate attack of the C6-hydroxyl group of the substrate on the thioester. Structure of the lac operon galactoside acetyltransferase.,Wang XG, Olsen LR, Roderick SL Structure. 2002 Apr;10(4):581-8. PMID:11937062[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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