pISSN 2288-6982
eISSN 2288-7105




BioDesign 2022; 10(2): 23-28

Published online June 30, 2022

© Korean Society for Structural Biology

Crystallization and X-ray crystallographic analysis of ribose 5-phosphate isomerase B in complex with its ligand from Vibrio vulnificus

Taek Hun Kwon1,2, Kyoungin Min2, Matthias Wolf3, Changill Ban2,* and Tae Gyun Kim3,4,*

1Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston 77030, TX, USA
2Department of Chemistry, Pohang University of Science and Technology, Pohang 37673, Republic of Korea
3Molecular Cryo-Electron Microscopy Unit, Okinawa Institute of Science and Technology Graduate University, Okinawa 904-0495, Japan
4Vaccine Commercialization Center, Gyeongbuk Institute for Bio Industry, Andong 33618, Republic of Korea

Correspondence to: *,

Received: February 15, 2022; Revised: May 10, 2022; Accepted: June 13, 2022


Ribose 5-phosphate isomerase is an enzyme that interconverts ribose 5-phosphate and ribulose 5-phosphate in the pentose phosphate pathway, which participates in NADPH generation, as well as an oxidative and non-oxidative synthesis of pentose sugars. Two distinct forms, ribose 5-phosphate isomerase A (RpiA) and ribose 5-phosphate isomerase B (RpiB), show no sequence identity even though they exist as ubiquitous, highly-conserved proteins in most kingdoms. RpiB from pathogenic, marine Vibrio vulnificus YJ016 (VvRpiB) was purified, crystallized, and analyzed to determine its structure in the apo form and in complex with a ligand. Crystals of the apo form of VvRpiB diffracted X-rays to 3.06 Å resolution, belonging to tetragonal space group I41 while co-crystals of VvRpiB with R5P belonged to the monoclinic space group C2 and diffracted X-rays to 2.07 Å resolution.