pISSN 2288-6982
eISSN 2288-7105




BioDesign 2021; 9(2): 41-45

Published online June 30, 2021

© Korean Society for Structural Biology

Purification and preliminary X-ray analysis of YbeY from Staphylococcus aureus

Jinwook Lee1, Aeran Kown2 and Nam-Chul Ha1,*

1Research Institute of Agriculture and Life Sciences, Center for Food and Bioconvergence, Department of Agricultural Biotechnology, CALS, Seoul National University, Seoul 08826, Republic of Korea
2Department of Beauty Care, College of Medical Science, Daegu Haany University, Gyeongsan 38610, Republic of Korea

Correspondence to: *

Received: May 29, 2021; Revised: June 10, 2021; Accepted: June 11, 2021


Endoribonuclease YbeY is essential for maturing ribosomal RNA in a wide range of bacteria. YbeY is specific to the single-stranded RNA of ribosomal RNAs and small RNAs. However, the structural relationship with the function and recognition of substrates remains elucidated. In this study, we overexpressed full-length YbeY from the gram-positive bacterium Staphylococcus aureus. The protein was purified and crystallized under conditions containing 0.1 M sodium citrate (pH 5.0) and 44% (w/v) polyethylene glycol 600. An X-ray diffraction dataset at a resolution of 1.9 Å was collected, and the dataset belonged to space group P63 with unit cell parameters a = 100.7 and c = 50.2 Å. The single-wavelength anomalous diffraction method was successful in determining the crystal structure. We are now refining the structure combined with structural analysis. The structure will provide molecular insights into the substrate recognition mechanism by showing the high-resolution features of the active sites.

Graphical Abstract