pISSN 2288-6982
eISSN 2288-7105




BioDesign 2023; 11(4): 66-69

Published online December 30, 2023

© Korean Society for Structural Biology

Preliminary crystallographic study of the molybdenum cofactor biosynthesis protein MocA complexed with CTP from Mycobacterium sp. strain JC1 DSM 3803

Ju Eun Lee1, Beom Sik Kang2,* and Hyo Je Cho1,*

1Department of Biochemistry, Chungbuk National University, Cheongju 28644, Republic of Korea
2School of Life Science and Biotechnology, BK21 Plus KNU Creative BioResearch Group, Kyungpook National University, Daegu 41566, Republic of Korea

Correspondence to: *,

Received: October 29, 2023; Revised: November 3, 2023; Accepted: November 6, 2023


In the biosynthesis of molybdopterin cytosine dinucleotide cofactor, MocA, molybdenum cofactor cytidylyltransferase, transfers the cytosine monophosphate moiety from cytosine triphosphate (CTP) to Mo-molybdopterin. In this study, we heterologously overexpressed MocA from Mycobacterium sp. strain JC1 DSM 3803 and purified the protein by Ni-NTA affinity and size-exclusion chromatography. The MocA protein was incubated with CTP and MnCl2, then crystallized under conditions containing 10% polyethylene glycol 6000 and 2 M sodium chloride. X-ray diffraction data were acquired at 1.55 Å resolution and belonged to the space group a P43212, with unit cell parameters a = 53.965 Å, b = 53.965 Å, c = 130.184 Å, and α = β = γ = 90°. An asymmetric unit of the crystal contains one MocA molecule with solvent content of 45.49% and Mathewes coefficient of 2.26 Å3/Da. A high-quality electron density map for the MocA complexed with CTP was obtained by a molecular replacement method.