3HGV

Structure of Phenazine Antibiotic Biosynthesis Protein

3HGV の概要

• エントリーDOI: 10.2210/pdb3hgv/pdb
• 関連するPDBエントリー: 3HGU
• 分子名称: EhpF (2 entities in total)
• 機能のキーワード: phenazine, antibiotic, biosynthetic protein
• 由来する生物種: Pantoea agglomerans (Erwinia herbicola)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 83121.52

構造登録者

Bera, A.K.,Atanasova, V.,Parsons, J.F. (登録日: 2009-05-14, 公開日: 2010-04-28, 最終更新日: 2024-10-30)

主引用文献

Bera, A.K.,Atanasova, V.,Gamage, S.,Robinson, H.,Parsons, J.F.
Structure of the D-alanylgriseoluteic acid biosynthetic protein EhpF, an atypical member of the ANL superfamily of adenylating enzymes.
Acta Crystallogr. D Biol. Crystallogr., 66:664-672, 2010

PubMed Abstract: The structure of EhpF, a 41 kDa protein that functions in the biosynthetic pathway leading to the broad-spectrum antimicrobial compound D-alanylgriseoluteic acid (AGA), is reported. A cluster of approximately 16 genes, including ehpF, located on a 200 kbp plasmid native to certain strains of Pantoea agglomerans encodes the proteins that are required for the conversion of chorismic acid to AGA. Phenazine-1,6-dicarboxylate has been identified as an intermediate in AGA biosynthesis and deletion of ehpF results in accumulation of this compound in vivo. The crystallographic data presented here reveal that EhpF is an atypical member of the acyl-CoA synthase or ANL superfamily of adenylating enzymes. These enzymes typically catalyze two-step reactions involving adenylation of a carboxylate substrate followed by transfer of the substrate from AMP to coenzyme A or another phosphopantetheine. EhpF is distinguished by the absence of the C-terminal domain that is characteristic of enzymes from this family and is involved in phosphopantetheine binding and in the second half of the canonical two-step reaction that is typically observed. Based on the structure of EhpF and a bioinformatic analysis, it is proposed that EhpF and EhpG convert phenazine-1,6-dicarboxylate to 6-formylphenazine-1-carboxylate via an adenylyl intermediate.

PubMed: 20516619
DOI: 10.1107/S0907444910008425

実験手法

X-RAY DIFFRACTION (2.3 Å)