1T4K

Crystal Structure of Unliganded Aldolase Antibody 93F3 Fab

1T4K の概要

• エントリーDOI: 10.2210/pdb1t4k/pdb
• 分子名称: IMMUNOGLOBULIN IGG1, KAPPA LIGHT CHAIN, IMMUNOGLOBULIN IGG1, HEAVY CHAIN, ZINC ION, ... (4 entities in total)
• 機能のキーワード: enantioselectivity, aldolase antibody, reactive lysine, aldol reaction, immune system
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 94471.15

構造登録者

Zhu, X.,Wilson, I.A. (登録日: 2004-04-29, 公開日: 2004-11-02, 最終更新日: 2024-10-30)

主引用文献

Zhu, X.,Tanaka, F.,Hu, Y.,Heine, A.,Fuller, R.,Zhong, G.,Olson, A.J.,Lerner, R.A.,Barbas, C.F.,Wilson, I.A.
The Origin of Enantioselectivity in Aldolase Antibodies: Crystal Structure, Site-directed Mutagenesis, and Computational Analysis
J.Mol.Biol., 343:1269-1280, 2004

PubMed Abstract: Catalytic aldolase antibodies, generated by reactive immunization, catalyze the aldol reaction with the efficiency of natural enzymes, but accept a much broader range of substrates. Two separate groups of aldolase antibodies that catalyze the same aldol reactions with antipodal selectivity were analyzed by comparing their amino acid sequences with their crystal structures, site-directed mutagenesis data, and computational docking of the transition states of the aldol reaction. The crystal structure of aldolase antibody 93F3 Fab' at 2.5A resolution revealed a combining site with two lysine residues, including LysL89 that reacts to form the covalent enamine intermediate. In contrast, antibody 33F12 has one active site lysine, LysH93. The reactive lysine residues in each group of antibodies are differentially located on the heavy and light chain variable regions in pseudo-symmetric opposite orientations, but both within highly hydrophobic environments. Thus, the defining feature for the observed enantioselectivities of these aldolase antibody catalysts is the respective location and relative disposition of the reactive lysine residues within the active sites of these catalysts.

PubMed: 15491612
DOI: 10.1016/j.jmb.2004.08.102

実験手法

X-RAY DIFFRACTION (2.5 Å)