6VV4

Scabin (V109G) toxin from Streptomyces scabies

6VV4 の概要

• エントリーDOI: 10.2210/pdb6vv4/pdb
• 分子名称: Scabin (2 entities in total)
• 機能のキーワード: transferase, toxin
• 由来する生物種: Streptomyces scabiei (strain 87.22)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21815.09

構造登録者

Heney, K.,Lyons, B.,Merrill, A.R. (登録日: 2020-02-16, 公開日: 2021-01-20, 最終更新日: 2023-10-11)

主引用文献

Vatta, M.,Lyons, B.,Heney, K.A.,Lidster, T.,Merrill, A.R.
Mapping the DNA-Binding Motif of Scabin Toxin, a Guanine Modifying Enzyme from Streptomyces scabies .
Toxins, 13:-, 2021

PubMed Abstract: Scabin is a mono-ADP-ribosyltransferase toxin/enzyme and possible virulence factor produced by the agriculture pathogen, . Recently, molecular dynamic approaches and MD simulations revealed its interaction with both NAD and DNA substrates. An Essential Dynamics Analysis identified a crab-claw-like mechanism, including coupled changes in the exposed motifs, and the R-R-N-STT-W-W-(QxE) sequence motif was proposed as a catalytic signature of the Pierisin family of DNA-acting toxins. A new fluorescence assay was devised to measure the kinetics for both RNA and DNA substrates. Several protein variants were prepared to probe the Scabin-NAD-DNA molecular model and to reveal the reaction mechanism for the transfer of ADP-ribose to the guanine base in the DNA substrate. The results revealed that there are several lysine and arginine residues in Scabin that are important for binding the DNA substrate; also, key residues such as Asn110 in the mechanism of ADP-ribose transfer to the guanine base were identified. The DNA-binding residues are shared with ScARP from but are not conserved with Pierisin-1, suggesting that the modification of guanine bases by ADP-ribosyltransferases is divergent even in the Pierisin family.

PubMed: 33450958
DOI: 10.3390/toxins13010055

実験手法

X-RAY DIFFRACTION (1.7 Å)