1krv
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Galactoside Acetyltransferase in Complex with CoA and PNP-beta-Gal
OverviewOverview
The 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.
About this StructureAbout this Structure
1KRV is a Single protein structure of sequence from Escherichia coli with 147 and COA as ligands. The following page contains interesting information on the relation of 1KRV with [lac Repressor]. Active as Galactoside O-acetyltransferase, with EC number 2.3.1.18 Full crystallographic information is available from OCA.
ReferenceReference
Structure of the lac operon galactoside acetyltransferase., Wang XG, Olsen LR, Roderick SL, Structure. 2002 Apr;10(4):581-8. PMID:11937062
Page seeded by OCA on Sun Nov 18 09:02:57 2007