1Q8F

Crystal Structure of the E.coli pyrimidine nucleoside hydrolase yeiK

Summary for 1Q8F

• Entry DOI: 10.2210/pdb1q8f/pdb
• Related: 1HP0 1MAS 2MAS
• Descriptor: Pyrimidine nucleoside hydrolase, CALCIUM ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: open alpha-beta structure, nh-fold, hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 4
• Total formula weight: 136681.22

Authors

Giabbai, B.,Degano, M. (deposition date: 2003-08-21, release date: 2004-05-11, Last modification date: 2023-08-16)

Primary citation

Giabbai, B.,Degano, M.
Crystal structure to 1.7 a of the Escherichia coli pyrimidine nucleoside hydrolase YeiK, a novel candidate for cancer gene therapy.
STRUCTURE, 12:739-749, 2004

PubMed Abstract: Enzymes with nucleoside hydrolase (NH) activity are crucial for salvaging nucleic acid components in purine auxotrophic protozoan parasites, but are also present in prokaryotes and higher eukaryotes. Here we analyze the distribution of genes encoding for putative NH proteins and characterize the yeiK gene product from Escherichia coli as a pyrimidine-specific NH. The crystal structure of YeiK to 1.7 A defines the structural basis for its substrate specificity and identifies residues involved in the catalytic mechanism that differ from both nonspecific and purine-specific NHs. Large differences in the tetrameric quaternary structure compared to nonspecific protozoan NHs are brought forth by minor differences in the interacting surfaces. The first structural and functional characterization of a nonparasitic, pyrimidine nucleoside-specific NH suggests a possible role for these enzymes in the metabolism of tRNA nucleosides. The high catalytic efficiency of YeiK toward 5-fluorouridine could be exploited for suicide gene therapy in cancer treatment.

PubMed: 15130467
DOI: 10.1016/j.str.2004.03.018

Experimental method

X-RAY DIFFRACTION (1.7 Å)