6FJH

Crystal structure of the seleniated LkcE from Streptomyces rochei

6FJH の概要

• エントリーDOI: 10.2210/pdb6fjh/pdb
• 関連するPDBエントリー: 6F32 6F7L 6F7V
• 分子名称: LkcE, FLAVIN-ADENINE DINUCLEOTIDE, OXYGEN MOLECULE, ... (5 entities in total)
• 機能のキーワード: amine oxydase, cyclase, post-pks enzyme, tayloring enzyme, flavoprotein
• 由来する生物種: Streptomyces rochei subsp. volubilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 101407.39

構造登録者

Dorival, J.,Risser, F.,Jacob, C.,Collin, S.,Drager, G.,Kirschning, A.,Paris, C.,Chagot, B.,Gruez, A.,Weissman, K.J. (登録日: 2018-01-22, 公開日: 2018-09-19, 最終更新日: 2024-10-23)

主引用文献

Dorival, J.,Risser, F.,Jacob, C.,Collin, S.,Drager, G.,Paris, C.,Chagot, B.,Kirschning, A.,Gruez, A.,Weissman, K.J.
Insights into a dual function amide oxidase/macrocyclase from lankacidin biosynthesis.
Nat Commun, 9:3998-3998, 2018

PubMed Abstract: Acquisition of new catalytic activity is a relatively rare evolutionary event. A striking example appears in the pathway to the antibiotic lankacidin, as a monoamine oxidase (MAO) family member, LkcE, catalyzes both an unusual amide oxidation, and a subsequent intramolecular Mannich reaction to form the polyketide macrocycle. We report evidence here for the molecular basis for this dual activity. The reaction sequence involves several essential active site residues and a conformational change likely comprising an interdomain hinge movement. These features, which have not previously been described in the MAO family, both depend on a unique dimerization mode relative to all structurally characterized members. Taken together, these data add weight to the idea that designing new multifunctional enzymes may require changes in both architecture and catalytic machinery. Encouragingly, however, our data also show LkcE to bind alternative substrates, supporting its potential utility as a general cyclization catalyst in synthetic biology.

PubMed: 30266997
DOI: 10.1038/s41467-018-06323-w

実験手法

X-RAY DIFFRACTION (3.15 Å)