1U5W

Crystal structure of hypothetical protein yjjX from Escherichia coli

Summary for 1U5W

• Entry DOI: 10.2210/pdb1u5w/pdb
• Descriptor: Hypothetical UPF0244 protein yjjX, SULFATE ION (3 entities in total)
• Functional Keywords: 3 layers alpha/beta/alpha protein, montreal-kingston bacterial structural genomics initiative, bsgi, structural genomics, unknown function
• Biological source: Escherichia coli
• Total number of polymer chains: 8
• Total formula weight: 161029.47

Authors

Zheng, J.,Singh, V.K.,Jia, Z.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2004-07-28, release date: 2005-08-23, Last modification date: 2024-02-14)

Primary citation

Zheng, J.,Singh, V.K.,Jia, Z.
Identification of an ITPase/XTPase in Escherichia coli by Structural and Biochemical Analysis
Structure, 13:1511-1520, 2005

PubMed Abstract: Inosine triphosphate (ITP) and xanthosine triphosphate (XTP) are formed upon deamination of ATP and GTP as a result of exposure to chemical mutagens and oxidative damage. Nucleic acid synthesis requires safeguard mechanisms to minimize undesired lethal incorporation of ITP and XTP. Here, we present the crystal structure of YjjX, a protein of hitherto unknown function. The three-dimensional fold of YjjX is similar to those of Mj0226 from Methanococcus janschii, which possesses nucleotidase activity, and of Maf from Bacillus subtilis, which can bind nucleotides. Biochemical analyses of YjjX revealed it to exhibit specific phosphatase activity for inosine and xanthosine triphosphates and have a possible interaction with elongation factor Tu. The enzymatic activity of YjjX as an inosine/xanthosine triphosphatase provides evidence for a plausible protection mechanism by clearing the noncanonical nucleotides from the cell during oxidative stress in E. coli.

PubMed: 16216582
DOI: 10.1016/j.str.2005.07.007

Experimental method

X-RAY DIFFRACTION (2.3 Å)