Gilliland, G.
(2008),
The 2.1- Crystal Structure of Haemophilus Influenzae HI1715, an Oligoribonuclease, Structure
(Accessed July 27, 2024)
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The 2.1- Crystal Structure of Haemophilus Influenzae HI1715, an Oligoribonuclease
Published
Author(s)
Abstract
The degradation of all classes of cellular RNA is critical for biological function. The enzymes that carry out this function in all organisms are either exo- or endo-specific ribonucleases. of the enzymes found in bacteria, oligoribonuclease is suggested to catalyze the final stages of polyribonucleotide degradation. In Escherichia coli this enzyme is the only ribonuclease that has been shown to be essential for viability. The homologous protein from Haemophilus influenzae, HI1715, has a 73% sequence identity to the E. coli enzyme and shows no significant amino acid sequence homology with other proteins in the Protein Data Bank.Citation
Structure
Pub Type
Journals
Keywords
oligoribonuclease, structural genomics
Citation
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Created October 16, 2008