6HTK

X-ray structure of the tryptophan lyase NosL in complex with (R)-(+)-indoline-2-carboxylate

6HTK の概要

• エントリーDOI: 10.2210/pdb6htk/pdb
• 分子名称: 3-methyl-2-indolic acid synthase, POTASSIUM ION, IRON/SULFUR CLUSTER, ... (11 entities in total)
• 機能のキーワード: radical sam, fes cluster, nosiheptide, antibiotic
• 由来する生物種: Streptomyces actuosus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 92944.76

構造登録者

Amara, P.,Mouesca, J.M.,Bella, M.,Martin, L.,Saragaglia, C.,Gambarelli, S.,Nicolet, Y. (登録日: 2018-10-04, 公開日: 2018-11-21, 最終更新日: 2025-12-10)

主引用文献

Amara, P.,Mouesca, J.M.,Bella, M.,Martin, L.,Saragaglia, C.,Gambarelli, S.,Nicolet, Y.
Radical S-Adenosyl-l-methionine Tryptophan Lyase (NosL): How the Protein Controls the Carboxyl Radical •CO2-Migration.
J.Am.Chem.Soc., 140:16661-16668, 2018

PubMed Abstract: The radical S-adenosyl-l-methionine tryptophan lyase uses radical-based chemistry to convert l-tryptophan into 3-methyl-2-indolic acid, a fragment in the biosynthesis of the thiopeptide antibiotic nosiheptide. This complex reaction involves several successive steps corresponding to (i) the activation by a specific hydrogen-atom abstraction, (ii) an unprecedented •CO radical migration, (iii) a cyanide fragment release, and (iv) the termination of the radical-based reaction. In vitro study of this reaction is made more difficult because the enzyme produces a significant amount of a shunt product instead of the natural product. Here, using a combination of X-ray crystallography, electron paramagnetic resonance spectroscopy, and quantum and hybrid quantum mechanical/molecular mechanical calculations, we have deciphered the fine mechanism of the key •CO radical migration, highlighting how the preorganized active site of the protein tightly controls this reaction.

PubMed: 30418774
DOI: 10.1021/jacs.8b09142

実験手法

X-RAY DIFFRACTION (2 Å)