3K0T

Crystal structure of PSPTO -PSP protein in complex with D-beta-Glucose from Pseudomonas syringae pv. tomato str. DC3000

Summary for 3K0T

• Entry DOI: 10.2210/pdb3k0t/pdb
• Descriptor: Endoribonuclease L-PSP, putative, beta-D-glucopyranose (3 entities in total)
• Functional Keywords: psp, glucose binding, er stressor, sugar binding protein
• Biological source: Pseudomonas syringae pv. tomato
• Total number of polymer chains: 3
• Total formula weight: 47646.28

Authors

Zhang, H.M.,Li, M.,Chang, W.R. (deposition date: 2009-09-25, release date: 2010-06-16, Last modification date: 2024-11-06)

Primary citation

Zhang, H.M.,Gao, Y.,Li, M.,Chang, W.R.
Crystal structure of the PSPTO-PSP protein from Pseudomonas syringae pv. tomato str. DC3000 in complex with D-glucose
Biochem.Biophys.Res.Commun., 397:82-86, 2010

PubMed Abstract: 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.

PubMed: 20478270
DOI: 10.1016/j.bbrc.2010.05.071

Experimental method

X-RAY DIFFRACTION (2.1 Å)