1q8f
From Proteopedia
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Crystal Structure of the E.coli pyrimidine nucleoside hydrolase yeiK
Overview
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.
About this Structure
1Q8F is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Ribosylpyrimidine nucleosidase, with EC number 3.2.2.8 Full crystallographic information is available from OCA.
Reference
Crystal structure to 1.7 a of the Escherichia coli pyrimidine nucleoside hydrolase YeiK, a novel candidate for cancer gene therapy., Giabbai B, Degano M, Structure. 2004 May;12(5):739-49. PMID:15130467
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