1krr | pdb_00001krr

Galactoside Acetyltransferase in Complex with Acetyl-Coenzyme A

spinqualitylabelsall models 1krr, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1krr is a 3 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACO Related: 1kqa, 1kru, 1krv Gene: lacA ("Bacillus coli" Migula 1895) Activity: Galactoside O-acetyltransferase, with EC number 2.3.1.18 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 PubMed 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. Structure of the lac operon galactoside acetyltransferase.,Wang XG, Olsen LR, Roderick SL Structure. 2002 Apr;10(4):581-8. PMID:11937062 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Galactoside O-acetyltransferase

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