7CCG

Crystal structure of ClA1, a kind of a chlorinase from soil bacteria

7CCG の概要

• エントリーDOI: 10.2210/pdb7ccg/pdb
• 分子名称: DNA-directed RNA polymerase subunit delta, METHIONINE, 5'-CHLORO-5'-DEOXYADENOSINE, ... (4 entities in total)
• 機能のキーワード: chlorinated enzyme, cla1, cell invasion
• 由来する生物種: Streptomyces albulus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28725.99

構造登録者

Ouyang, Z.,Li, Y. (登録日: 2020-06-17, 公開日: 2020-09-09, 最終更新日: 2023-11-29)

主引用文献

Miao, Y.,Yu, J.,Ouyang, Z.,Sun, H.,Li, Y.
Crystal structure of ClA1, a type of chlorinase from soil bacteria.
Biochem.Biophys.Res.Commun., 530:42-46, 2020

PubMed Abstract: Halogenated compounds are widely discovered in nature, and many of them exhibit biological activities, such as an important chlorinated natural product salinosporamide A serving as a potential anticancer agent. Compared with bromination, iodination and fluorination, chlorination is the mainly important modification. To shed light on the mechanism of SAM-dependent chlorinases, a recombinant chlorinase ClA1 was expressed in Escherichia coli and further purified for crystallization and X-ray diffraction experiments. The flake crystals of ClA1 were able to diffract to a resolution of 1.85 Å. The crystals belonged to space group R3, with unit-cell parameters α = β = 90.0°, γ = 120.0°. By determining the structure of ClA1, it is revealed that the side chain of Arg242 in ClA1 may have contacts with the L-Met. However, in SalL the equivalent Arg243's side chain is far from L-Met. Considering the ClA1 and SalL are from different environments and their enzyme kinetics are quite different, it is suggested that the side chain conformation differences of the conserved arginine are possibly related with the enzyme activity differences of the two chlorinases.

PubMed: 32828313
DOI: 10.1016/j.bbrc.2020.06.129

実験手法

X-RAY DIFFRACTION (1.85 Å)