5EY2

Crystal structure of CodY from Bacillus cereus

Summary for 5EY2

• Entry DOI: 10.2210/pdb5ey2/pdb
• Related: 5EY0 5EY1
• Descriptor: GTP-sensing transcriptional pleiotropic repressor CodY (2 entities in total)
• Functional Keywords: gtp-sensing, pleiotropic transcription regulator, auto-inhibition, transcription
• Biological source: Bacillus cereus (strain ATCC 14579 / DSM 31)
• Total number of polymer chains: 4
• Total formula weight: 124744.81

Authors

Han, A.,Lee, W.C.,Son, J.,Kim, S.H.,Hwang, K.Y. (deposition date: 2015-11-24, release date: 2016-09-14, Last modification date: 2024-10-23)

Primary citation

Han, A.R.,Kang, H.R.,Son, J.,Kwon, D.H.,Kim, S.,Lee, W.C.,Song, H.K.,Song, M.J.,Hwang, K.Y.
The structure of the pleiotropic transcription regulator CodY provides insight into its GTP-sensing mechanism
Nucleic Acids Res., 44:9483-9493, 2016

PubMed Abstract: GTP and branched-chain amino acids (BCAAs) are metabolic sensors that are indispensable for the determination of the metabolic status of cells. However, their molecular sensing mechanism remains unclear. CodY is a unique global transcription regulator that recognizes GTP and BCAAs as specific signals and affects expression of more than 100 genes associated with metabolism. Herein, we report the first crystal structures of the full-length CodY complex with sensing molecules and describe their functional states. We observed two different oligomeric states of CodY: a dimeric complex of CodY from Staphylococcus aureus with the two metabolites GTP and isoleucine, and a tetrameric form (apo) of CodY from Bacillus cereus Notably, the tetrameric state shows in an auto-inhibitory manner by blocking the GTP-binding site, whereas the binding sites of GTP and isoleucine are clearly visible in the dimeric state. The GTP is located at a hinge site between the long helical region and the metabolite-binding site. Together, data from structural and electrophoretic mobility shift assay analyses improve understanding of how CodY senses GTP and operates as a DNA-binding protein and a pleiotropic transcription regulator.

PubMed: 27596595
DOI: 10.1093/nar/gkw775

Experimental method

X-RAY DIFFRACTION (3 Å)