7CNR

Crystal structure of Thermococcus kodakaraensis aconitase X (apo-form)

7CNR の概要

• エントリーDOI: 10.2210/pdb7cnr/pdb
• 分子名称: DUF521 domain-containing protein, UPF0107 protein TK1248, FE3-S4 CLUSTER (3 entities in total)
• 機能のキーワード: mevalonate 5-phosphate dehydratase, lyase
• 由来する生物種: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 226460.58

構造登録者

Murase, Y.,Watanabe, Y.,Watanabe, S. (登録日: 2020-08-03, 公開日: 2021-06-16, 最終更新日: 2024-05-29)

主引用文献

Watanabe, S.,Murase, Y.,Watanabe, Y.,Sakurai, Y.,Tajima, K.
Crystal structures of aconitase X enzymes from bacteria and archaea provide insights into the molecular evolution of the aconitase superfamily.
Commun Biol, 4:687-687, 2021

PubMed Abstract: Aconitase superfamily members catalyze the homologous isomerization of specific substrates by sequential dehydration and hydration and contain a [4Fe-4S] cluster. However, monomeric and heterodimeric types of function unknown aconitase X (AcnX) have recently been characterized as a cis-3-hydroxy-L-proline dehydratase (AcnX) and mevalonate 5-phosphate dehydratase (AcnX), respectively. We herein elucidated the crystal structures of AcnX from Agrobacterium tumefaciens (AtAcnX) and AcnX from Thermococcus kodakarensis (TkAcnX) without a ligand and in complex with substrates. AtAcnX and TkAcnX contained the [2Fe-2S] and [3Fe-4S] clusters, respectively, conforming to UV and EPR spectroscopy analyses. The binding sites of the [Fe-S] cluster and substrate were clearlydifferent from those that were completely conserved in other aconitase enzymes; however, theoverall structural frameworks and locations of active sites were partially similar to each other.These results provide novel insights into the evolutionary scenario of the aconitase superfamilybased on the recruitment hypothesis.

PubMed: 34099860
DOI: 10.1038/s42003-021-02147-5

実験手法

X-RAY DIFFRACTION (3.39 Å)