7CPN

CRYSTAL STRUCTURE OF DODECAPRENYL DIPHOSPHATE SYNTHASE FROM THERMOBIFIDA FUSCA

7CPN の概要

• エントリーDOI: 10.2210/pdb7cpn/pdb
• 関連するPDBエントリー: 7CPM
• 分子名称: Trans,polycis-polyprenyl diphosphate synthase ((2Z,6E)-farnesyl diphosphate specific), GLYCEROL, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: prenyltransferase, transferase
• 由来する生物種: Thermobifida fusca (strain YX)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 193431.54

構造登録者

Kurokawa, H.,Ambo, T.,Takahasi, S.,Koyama, T. (登録日: 2020-08-07, 公開日: 2020-10-14, 最終更新日: 2023-11-29)

主引用文献

Kurokawa, H.,Ambo, T.,Takahashi, S.,Koyama, T.
Crystal structure of Thermobifida fusca cis-prenyltransferase reveals the dynamic nature of its RXG motif-mediated inter-subunit interactions critical for its catalytic activity.
Biochem.Biophys.Res.Commun., 532:459-465, 2020

PubMed Abstract: cis-Prenyltransferases (cis-PTs) catalyze consecutive condensations of isopentenyl diphosphate to an allylic diphosphate acceptor to produce a linear polyprenyl diphosphate of designated length. Dimer formation is a prerequisite for cis-PTs to catalyze all cis-prenyl condensation reactions. The structure-function relationship of a conserved C-terminal RXG motif in cis-PTs that forms inter-subunit interactions and has a role in catalytic activity has attracted much attention. Here, we solved the crystal structure of a medium-chain cis-PT from Thermobifida fusca that produces dodecaprenyl diphosphate as a polyprenoid glycan carrier for cell wall synthesis. The structure revealed a characteristic dimeric architecture of cis-PTs in which a rigidified RXG motif of one monomer formed inter-subunit hydrogen bonds with the catalytic site of the other monomer, while the RXG motif of the latter remained flexible. Careful analyses suggested the existence of a possible long-range negative cooperativity between the two catalytic sites on the two monomeric subunits that allowed the binding of one subunit to stabilize the formation of the enzyme-substrate ternary complex and facilitated the release of Mg-PPi and subsequent intra-molecular translocation at the counter subunit so that the condensation reaction could occur in consecutive cycles. The current structure reveals the dynamic nature of the RXG motif and provides a rationale for pursuing further investigations to elucidate the inter-subunit cooperativity of cis-PTs.

PubMed: 32892948
DOI: 10.1016/j.bbrc.2020.08.062

実験手法

X-RAY DIFFRACTION (2.28 Å)