3k0t

Publication Abstract from PubMed

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.

Crystal structure of the PSPTO-PSP protein from Pseudomonas syringae pv. tomato str. DC3000 in complex with D-glucose.,Zhang HM, Gao Y, Li M, Chang WR Biochem Biophys Res Commun. 2010 Jun 18;397(1):82-6. Epub 2010 May 15. PMID:20478270^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.