4CKD

Model of complex between the E.coli enzyme beta-galactosidase and four single chain Fv antibody domains scFv13R4.

4CKD の概要

• エントリーDOI: 10.2210/pdb4ckd/pdb
• EMDBエントリー: 2548
• 分子名称: BETA-GALACTOSIDASE, SCFV13R4 ANTIBODY FV HEAVY CHAIN, SCFV13R4 ANTIBODY FV LIGHT CHAIN (3 entities in total)
• 機能のキーワード: hydrolase-immune system complex, hydrolase/immune system
• 由来する生物種: ESCHERICHIA COLI K-12; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 564092.87

構造登録者

Vinothkumar, K.R.,McMullan, G.,Henderson, R. (登録日: 2014-01-03, 公開日: 2014-01-15, 最終更新日: 2024-10-16)

主引用文献

Vinothkumar, K.R.,Mcmullan, G.,Henderson, R.
Molecular Mechanism of Antibody-Mediated Activation of Beta-Galactosidase.
Structure, 22:621-, 2014

PubMed Abstract: Binding of a single-chain Fv antibody to Escherichia coli β-galactosidase (β-gal) is known to stabilize the enzyme and activate several inactive point mutants, historically called antibody-mediated enzyme formation mutants. To understand the nature of this activation, we have determined by electron cryo-microscopy the structure of the complex between β-gal and the antibody scFv13R4. Our structure localizes the scFv13R4 binding site to the crevice between domains 1 and 3 in each β-gal subunit. The mutations that scFv13R4 counteracts are located between the antibody binding site and the active site of β-gal, at one end of the TIM-barrel that forms domain 3 where the substrate lactose is hydrolyzed. The mode of binding suggests how scFv stabilizes both the active site of β-gal and the tetrameric state.

PubMed: 24613486
DOI: 10.1016/J.STR.2014.01.011

実験手法

ELECTRON MICROSCOPY (13 Å)