1KQA

GALACTOSIDE ACETYLTRANSFERASE IN COMPLEX WITH COENZYME A

1KQA の概要

• エントリーDOI: 10.2210/pdb1kqa/pdb
• 関連するPDBエントリー: 1KRR 1KRU 1KRV
• 分子名称: GALACTOSIDE O-ACETYLTRANSFERASE, COENZYME A (2 entities in total)
• 機能のキーワード: left-handed parallel beta helix, transferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P07464
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 70783.60

構造登録者

Wang, X.-G.,Olsen, L.R.,Roderick, S.L. (登録日: 2002-01-04, 公開日: 2002-04-10, 最終更新日: 2024-02-14)

主引用文献

Wang, X.G.,Olsen, L.R.,Roderick, S.L.
Structure of the lac operon galactoside acetyltransferase.
Structure, 10:581-588, 2002

PubMed Abstract: 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.

PubMed: 11937062
DOI: 10.1016/S0969-2126(02)00741-4

実験手法

X-RAY DIFFRACTION (3.2 Å)