4CW5

Crystal structure of the enoyl reductase domain of DfnA from Bacillus amyloliquefaciens

4CW5 の概要

• エントリーDOI: 10.2210/pdb4cw5/pdb
• 関連するPDBエントリー: 4CW4
• 分子名称: DFNA, FLAVIN MONONUCLEOTIDE (3 entities in total)
• 機能のキーワード: oxidoreductase, trans-at pks, polyketide
• 由来する生物種: BACILLUS AMYLOLIQUEFACIENS FZB42
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 103079.25

構造登録者

Jakob, R.P.,Buhkari, H.S.T.,Maier, T. (登録日: 2014-04-01, 公開日: 2014-12-17, 最終更新日: 2024-10-23)

主引用文献

Bukhari, H.S.,Jakob, R.P.,Maier, T.
Evolutionary Origins of the Multienzyme Architecture of Giant Fungal Fatty Acid Synthase.
Structure, 22:1775-, 2014

PubMed Abstract: Fungal fatty acid synthase (fFAS) is a key paradigm for the evolution of complex multienzymes. Its 48 functional domains are embedded in a matrix of scaffolding elements, which comprises almost 50% of the total sequence and determines the emergent multienzymes properties of fFAS. Catalytic domains of fFAS are derived from monofunctional bacterial enzymes, but the evolutionary origin of the scaffolding elements remains enigmatic. Here, we identify two bacterial protein families of noncanonical fatty acid biosynthesis starter enzymes and trans-acting polyketide enoyl reductases (ERs) as potential ancestors of scaffolding regions in fFAS. The architectures of both protein families are revealed by representative crystal structures of the starter enzyme FabY and DfnA-ER. In both families, a striking structural conservation of insertions to scaffolding elements in fFAS is observed, despite marginal sequence identity. The combined phylogenetic and structural data provide insights into the evolutionary origins of the complex multienzyme architecture of fFAS.

PubMed: 25456814
DOI: 10.1016/J.STR.2014.09.016

実験手法

X-RAY DIFFRACTION (2.3 Å)