6SLS

Flavin-dependent tryptophan 6-halogenase Thal in complex with FAD

6SLS の概要

• エントリーDOI: 10.2210/pdb6sls/pdb
• 関連するPDBエントリー: 6H43 6H44 6IB5 6SLT
• 分子名称: Tryptophan 6-halogenase, GLYCEROL, PHOSPHATE ION, ... (6 entities in total)
• 機能のキーワード: tryptophan halogenase, thdh, flavoprotein, thal, fad
• 由来する生物種: Streptomyces albogriseolus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 122915.30

構造登録者

Moritzer, A.,Niemann, H.H. (登録日: 2019-08-20, 公開日: 2019-10-16, 最終更新日: 2024-01-24)

主引用文献

Moritzer, A.C.,Niemann, H.H.
Binding of FAD and tryptophan to the tryptophan 6-halogenase Thal is negatively coupled.
Protein Sci., 28:2112-2118, 2019

PubMed Abstract: Flavin-dependent halogenases require reduced flavin adenine dinucleotide (FADH ), O , and halide salts to halogenate their substrates. We describe the crystal structures of the tryptophan 6-halogenase Thal in complex with FAD or with both tryptophan and FAD. If tryptophan and FAD were soaked simultaneously, both ligands showed impaired binding and in some cases only the adenosine monophosphate or the adenosine moiety of FAD was resolved, suggesting that tryptophan binding increases the mobility mainly of the flavin mononucleotide moiety. This confirms a negative cooperativity between the binding of substrate and cofactor that was previously described for other tryptophan halogenases. Binding of substrate to tryptophan halogenases reduces the affinity for the oxidized cofactor FAD presumably to facilitate the regeneration of FADH by flavin reductases.

PubMed: 31589794
DOI: 10.1002/pro.3739

実験手法

X-RAY DIFFRACTION (2.32 Å)