7QC9

HisF-C9A-D11E-V33A_L50H_I52H mutant in complex with Ni(II) from T. maritima

7QC9 の概要

• エントリーDOI: 10.2210/pdb7qc9/pdb
• 関連するPDBエントリー: 2A0N
• 分子名称: Imidazole glycerol phosphate synthase subunit HisF, NICKEL (II) ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: beta barrel, artificial metalloenzyme, protein design, oxidoreductase, metal binding protein
• 由来する生物種: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28082.65

構造登録者

Beaumet, M.,Dose, A.,Braeuer, A.,Mahy, J.,Ghattas, W.,Groll, M.,Hess, C. (登録日: 2021-11-22, 公開日: 2022-08-10, 最終更新日: 2024-01-31)

主引用文献

Beaumet, M.,Dose, A.,Brauer, A.,Mahy, J.P.,Ghattas, W.,Groll, M.,Hess, C.R.
An artificial metalloprotein with metal-adaptive coordination sites and Ni-dependent quercetinase activity.
J.Inorg.Biochem., 235:111914-111914, 2022

PubMed Abstract: Engineering non-native metal active sites into proteins using canonical amino acids offers many advantages but is hampered by significant challenges. The TIM barrel protein, imidazole glycerol phosphate synthase from the hyperthermophilic organism Thermotoga maritima (tHisF), is well-suited for the construction of artificial metalloenzymes by this approach. To this end, we have generated a tHisF variant (tHisF) with a Glu/His/His motif for metal ion coordination. Crystal structures of Zn:tHisF and Ni:tHisF reveal that both metal ions bind to the engineered histidines. However, the two metals bind at distinct sites with different geometries, demonstrating the adaptability of tHisF. Only Zn additionally ligates the Glu residue and adopts a tetrahedral geometry. The pseudo-octahedral Ni site comprises the two His and a native Ser residue. Ni:tHisF catalyzes the oxidative cleavage of the flavanols quercetin and myricetin, providing an unprecedented example of an artificial metalloprotein with quercetinase activity.

PubMed: 35841720
DOI: 10.1016/j.jinorgbio.2022.111914

実験手法

X-RAY DIFFRACTION (1.8 Å)