Crystal structure of the PSPTO-PSP protein from Pseudomonas syringae pv. tomato str. DC3000 in complex with D-glucose.
The perchloric acid-soluble protein (PSP) is an endoribonuclease and on the basis of sequence similarity has been assigned to the YjgF/YER057c/UK114 family. These family members are ubiquitous and highly conserved in evolution, and participate in regulating basic cellular metabolism. Here we present the 2.1A crystal structure of the PSP protein from Pseudomonas syringae pv. tomato str. DC3000 (PSPTO-PSP), in complex with D-glucose. The quaternary structure of PSPTO-PSP is a homologous trimer. Glucose is located in the cavity between each two monomers. Comparison of the hydrogen bonds between ligands and YjgF/YER057c/UK114 family homologues confirms that the conserved Arg(103) of PSPTO-PSP is a key amino acid in this cavity for ligand binding. It indicated that the involvement of PSPTO-PSP in essential cellular mechanism was regulated by glucose occupying this active site.
Zhang
Hong-mei
HM
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing, PR China.
Gao
Yu
Y
Li
Mei
M
Chang
Wen-rui
WR
D001665:Binding Sites; D018360:Crystallography, X-Ray; D005947:Glucose / Q000737:chemistry*; D006360:Heat-Shock Proteins / Q000737:chemistry*; D006860:Hydrogen Bonding; D044224:Pseudomonas syringae / Q000378:metabolism*
D006360:Heat-Shock Proteins; D005947:Glucose