5E0K

X-ray crystal structure of tryptophan synthase complex from Pyrococcus furiosus at 2.76 A

5E0K の概要

• エントリーDOI: 10.2210/pdb5e0k/pdb
• 関連するPDBエントリー: 5DVZ 5DW0 5DW3
• 分子名称: Tryptophan synthase alpha chain, Tryptophan synthase beta chain 1, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: complex, plp, lyase, enzyme
• 由来する生物種: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 429095.17

構造登録者

Buller, A.R.,Murciano-Calles, J.,Arnold, F.H. (登録日: 2015-09-29, 公開日: 2015-11-11, 最終更新日: 2025-04-02)

主引用文献

Buller, A.R.,Brinkmann-Chen, S.,Romney, D.K.,Herger, M.,Murciano-Calles, J.,Arnold, F.H.
Directed evolution of the tryptophan synthase beta-subunit for stand-alone function recapitulates allosteric activation.
Proc.Natl.Acad.Sci.USA, 112:14599-14604, 2015

PubMed Abstract: Enzymes in heteromeric, allosterically regulated complexes catalyze a rich array of chemical reactions. Separating the subunits of such complexes, however, often severely attenuates their catalytic activities, because they can no longer be activated by their protein partners. We used directed evolution to explore allosteric regulation as a source of latent catalytic potential using the β-subunit of tryptophan synthase from Pyrococcus furiosus (PfTrpB). As part of its native αββα complex, TrpB efficiently produces tryptophan and tryptophan analogs; activity drops considerably when it is used as a stand-alone catalyst without the α-subunit. Kinetic, spectroscopic, and X-ray crystallographic data show that this lost activity can be recovered by mutations that reproduce the effects of complexation with the α-subunit. The engineered PfTrpB is a powerful platform for production of Trp analogs and for further directed evolution to expand substrate and reaction scope.

PubMed: 26553994
DOI: 10.1073/pnas.1516401112

実験手法

X-RAY DIFFRACTION (2.76 Å)