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

• 영문명: Preliminary crystallographic study of the molybdenum cofactor biosynthesis protein MocA complexed with CTP from Mycobacterium sp. strain JC1 DSM 3803
• 발행기관: 한국구조생물학회
• 저자명: Ju Eun Lee Beom Sik Kang Hyo Je Cho
• 간행물 정보: 『Biodesign』Vol 11, No 4, Dec, 66~69쪽, 전체 4쪽
• 주제분류: 자연과학 > 생물학
• 파일형태: PDF
• 발행일자: 2023.12.31

영문 초록

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.

목차

INTRODUCTION

RESULTS AND DISCUSSION

METHODS

X-ray diffraction analysis of MocA

ACKNOWLEDGEMENTS

CONFLICT OF INTEREST

REFERENCES