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Crystal structure of the YajQ protein from Haemophilus influenzae reveals a tandem of RNP-like domains



A Teplyakov, G Obmolova, Prasad T. Reddy, A J. Howard, G L. Gilliland


A hypothetical protein encoded by the gene YajQ of Haemophilus influenzae was selected, as part of a structural genomics project, for x-ray crystallographic structure determination and analysis to assist with the functional assignment. The protein is considered essential to bacteria since the gene is present in most bacterial genomes, but not in those of archaea or eukaryotes. The amino acid sequence has no homology to that of other proteins. The YajQ protein was cloned, expressed, and the crystal structure determined at 2.1 resolution by applying the multiwavelength anomalous dispersion method to a mercury derivative. The polypeptide chain is folded into two domains with identical folding topology. Each domain has a four-stranded antiparallel b-sheet flanked on one side by two a-helices. This structural motif is a characteristic feature of many RNA-binding proteins. The tetrameric structure observed in the crystal suggests a possibility of binding two stretches of double-stranded nucleic acid.
Journal of Structural and Functional Genomics


haemophilus influenzae, RNP-like domain, structural geonomics, tandem repeat, three-dimensional structure


Teplyakov, A. , Obmolova, G. , Reddy, P. , Howard, A. and Gilliland, G. (2003), Crystal structure of the YajQ protein from Haemophilus influenzae reveals a tandem of RNP-like domains, Journal of Structural and Functional Genomics (Accessed July 17, 2024)


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Created January 1, 2003, Updated February 17, 2017