Crystal structure of red sea bream transglutaminase

被引:74
作者
Noguchi, K
Ishikawa, K
Yokoyama, K
Ohtsuka, T
Nio, N
Suzuki, E
机构
[1] Ajinomoto Co Inc, Cent Res Labs, Kawasaki Ku, Kawasaki, Kanagawa 2108681, Japan
[2] Ajinomoto Co Inc, Food Res & Dev Labs, Kawasaki Ku, Kawasaki, Kanagawa 2108681, Japan
关键词
D O I
10.1074/jbc.M009862200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The crystal structure of the tissue-type transglutaminase from red sea bream liver (fish-derived transglutaminase, FTG) has been determined at 2.5-Angstrom resolution using the molecular replacement method, based on the crystal structure of human blood coagulation factor XIIII, which is a transglutaminase zymogen. The model contains 666 residues of a total of 695 residues, 382 water molecules, and 1 sulfate ion. FTG consists of four domains, and its overall and active site structures are similar to those of human factor XIII, However, significant structural differences are observed in both the acyl do nor and acyl acceptor binding sites, which account for the difference in substrate preferences. The active site of the enzyme is inaccessible to the solvent, because the catalytic Cys-272 hydrogen-bonds to Tyr-515, which is thought to be displaced upon acyl donor binding to FTG. It is postulated that the binding of an inappropriate substrate to FTG would lead to inactivation of the enzyme because of the formation of a new disulfide bridge between Cys-272 and the adjacent Cys-333 immediately after the displacement of Tyr-515. Considering the mutational studies previously reported on the tissue-type transglutaminases, we propose that Cys-333 and Tyr-515 are important in strictly controlling the enzymatic activity of FTG.
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页码:12055 / 12059
页数:5
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