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3L2K

Structure of phenazine antibiotic biosynthesis protein with substrate

3L2K の概要
エントリーDOI10.2210/pdb3l2k/pdb
関連するPDBエントリー3HGU 3HGV
分子名称EhpF, phenazine-1,6-dicarboxylic acid (3 entities in total)
機能のキーワードphenazine, antibiotic, biosynthetic protein, pdc
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82343.11
構造登録者
Bera, A.K.,Atanasova, V.,Parsons, J.F. (登録日: 2009-12-15, 公開日: 2010-05-26, 最終更新日: 2023-09-06)
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.,Sect.D, 66:664-672, 2010
Cited by
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.8 Å)
構造検証レポート
Validation report summary of 3l2k
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-11に公開中

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