7PD1

Crystal structure of the L-tyrosine-bound radical SAM tyrosine lyase ThiH (2-iminoacetate synthase) from Thermosinus carboxydivorans

7PD1 の概要

• エントリーDOI: 10.2210/pdb7pd1/pdb
• 分子名称: Thiazole biosynthesis protein ThiH, IRON/SULFUR CLUSTER, 5'-DEOXYADENOSINE, ... (10 entities in total)
• 機能のキーワード: radical sam enzyme 2-iminoacetate metalloprotein, lyase
• 由来する生物種: Thermosinus carboxydivorans Nor1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 89427.16

構造登録者

Amara, P.,Saragaglia, C.,Mouesca, J.-M.,Martin, L.,Nicolet, Y. (登録日: 2021-08-04, 公開日: 2022-05-11, 最終更新日: 2024-01-31)

主引用文献

Amara, P.,Saragaglia, C.,Mouesca, J.M.,Martin, L.,Nicolet, Y.
L-tyrosine-bound ThiH structure reveals C-C bond break differences within radical SAM aromatic amino acid lyases.
Nat Commun, 13:2284-2284, 2022

PubMed Abstract: 2-iminoacetate synthase ThiH is a radical S-adenosyl-L-methionine (SAM) L-tyrosine lyase and catalyzes the L-tyrosine Cα-Cβ bond break to produce dehydroglycine and p-cresol while the radical SAM L-tryptophan lyase NosL cleaves the L-tryptophan Cα-C bond to produce 3-methylindole-2-carboxylic acid. It has been difficult to understand the features that condition one C-C bond break over the other one because the two enzymes display significant primary structure similarities and presumably similar substrate-binding modes. Here, we report the crystal structure of L-tyrosine bound ThiH from Thermosinus carboxydivorans revealing an unusual protonation state of L-tyrosine upon binding. Structural comparison of ThiH with NosL and computational studies of the respective reactions they catalyze show that substrate activation is eased by tunneling effect and that subtle structural changes between the two enzymes affect, in particular, the hydrogen-atom abstraction by the 5´-deoxyadenosyl radical species, driving the difference in reaction specificity.

PubMed: 35477710
DOI: 10.1038/s41467-022-29980-4

実験手法

X-RAY DIFFRACTION (1.27 Å)