Next Article in Journal
Dynamics of Dislocations in Smectic A Liquid Crystals Doped with Nanoparticles
Next Article in Special Issue
Structural Analyses of Helicobacter Pylori FolC Conducting Glutamation in Folate Metabolism
Previous Article in Journal
Monte Carlo Optical Simulations of a Small FoV Gamma Camera. Effect of Scintillator Thicknesses and Septa Materials
Open AccessArticle

Crystal Structure of Chaperonin GroEL from Xanthomonas oryzae pv. oryzae

1
Department of Biological Sciences, Konkuk University, 120 Neungdong-ro, Gwangjin-gu, Seoul 05029, Korea
2
Genomics Division, National Institute of Agricultural Sciences, Rural Development Administration (RDA), Jeonju 03016, Korea
3
Department of Biotechnology, Sangmyung University, 20 Hongji-dong 2-gil, Jongno-gu, Seoul 03016, Korea
*
Author to whom correspondence should be addressed.
These authors contributed equally to this paper.
Crystals 2019, 9(8), 399; https://doi.org/10.3390/cryst9080399
Received: 16 July 2019 / Revised: 28 July 2019 / Accepted: 28 July 2019 / Published: 2 August 2019
(This article belongs to the Special Issue Crystallographic Studies of Enzymes)
Xanthomonas oryzae pv. oryzae (Xoo) is a plant pathogen that causes bacterial blight of rice, with outbreaks occurring in most rice-growing countries. Thus far, there is no effective pesticide against bacterial blight. Chaperones in bacterial pathogens are important for the stabilization and delivery of effectors into host cells to cause disease. In bacteria, GroEL/GroES complex mediates protein folding and protects proteins against misfolding and aggregation caused by environmental stress. We determined the crystal structure of GroEL from Xanthomonas oryzae pv. oryzae (XoGroEL) at 3.2 Å resolution, which showed the open form of two conserved homoheptameric rings stacked back-to-back. In the open form structure, the apical domain of XoGroEL had a higher B factor than the intermediate and equatorial domains, indicating that the apical domain had a flexible conformation before the binding of substrate unfolded protein and ATP. The XoGroEL structure will be helpful in understanding the function and catalytic mechanism of bacterial chaperonin GroELs. View Full-Text
Keywords: GroEL; chaperonin; Xanthomonas oryzae pv. oryzae (Xoo); protein crystallography GroEL; chaperonin; Xanthomonas oryzae pv. oryzae (Xoo); protein crystallography
Show Figures

Graphical abstract

MDPI and ACS Style

Tran, H.-T.; Lee, J.; Park, H.; Kim, J.-G.; Kim, S.; Ahn, Y.-J.; Kang, L.-W. Crystal Structure of Chaperonin GroEL from Xanthomonas oryzae pv. oryzae. Crystals 2019, 9, 399. https://doi.org/10.3390/cryst9080399

AMA Style

Tran H-T, Lee J, Park H, Kim J-G, Kim S, Ahn Y-J, Kang L-W. Crystal Structure of Chaperonin GroEL from Xanthomonas oryzae pv. oryzae. Crystals. 2019; 9(8):399. https://doi.org/10.3390/cryst9080399

Chicago/Turabian Style

Tran, Huyen-Thi; Lee, Jongha; Park, Hyunjae; Kim, Jeong-Gu; Kim, Seunghwan; Ahn, Yeh-Jin; Kang, Lin-Woo. 2019. "Crystal Structure of Chaperonin GroEL from Xanthomonas oryzae pv. oryzae" Crystals 9, no. 8: 399. https://doi.org/10.3390/cryst9080399

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop