1LTA
2.2 ANGSTROMS CRYSTAL STRUCTURE OF E. COLI HEAT-LABILE ENTEROTOXIN (LT) WITH BOUND GALACTOSE
1LTA の概要
| エントリーDOI | 10.2210/pdb1lta/pdb |
| 分子名称 | HEAT-LABILE ENTEROTOXIN, SUBUNIT B, HEAT-LABILE ENTEROTOXIN, SUBUNIT A, beta-D-galactopyranose, ... (5 entities in total) |
| 機能のキーワード | enterotoxin |
| 由来する生物種 | Escherichia coli 詳細 |
| タンパク質・核酸の鎖数 | 7 |
| 化学式量合計 | 87519.82 |
| 構造登録者 | Merritt, E.A.,Sixma, T.K.,Kalk, K.H.,Van Zanten, B.A.M.,Hol, W.G.J. (登録日: 1993-09-15, 公開日: 1994-01-31, 最終更新日: 2024-11-06) |
| 主引用文献 | Merritt, E.A.,Sixma, T.K.,Kalk, K.H.,van Zanten, B.A.,Hol, W.G. Galactose-binding site in Escherichia coli heat-labile enterotoxin (LT) and cholera toxin (CT). Mol.Microbiol., 13:745-753, 1994 Cited by PubMed Abstract: The galactose-binding site in cholera toxin and the closely related heat-labile enterotoxin (LT) from Escherichia coli is an attractive target for the rational design of potential anti-cholera drugs. In this paper we analyse the molecular structure of this binding site as seen in several crystal structures, including that of an LT:galactose complex which we report here at 2.2 A resolution. The binding surface on the free toxin contains several tightly associated water molecules and a relatively flexible loop consisting of residues 51-60 of the B subunit. During receptor binding this loop becomes tightly ordered by forming hydrogen bonds jointly to the GM1 pentasaccharide and to a set of water molecules which stabilize the toxin:receptor complex. PubMed: 7997185DOI: 10.1111/j.1365-2958.1994.tb00467.x 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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