7CCG

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

Summary for 7CCG

• Entry DOI: 10.2210/pdb7ccg/pdb
• Descriptor: DNA-directed RNA polymerase subunit delta, METHIONINE, 5'-CHLORO-5'-DEOXYADENOSINE, ... (4 entities in total)
• Functional Keywords: chlorinated enzyme, cla1, cell invasion
• Biological source: Streptomyces albulus
• Total number of polymer chains: 1
• Total formula weight: 28725.99

Authors

Ouyang, Z.,Li, Y. (deposition date: 2020-06-17, release date: 2020-09-09, Last modification date: 2023-11-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.85 Å)