This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. LysN is a 120 residue polypeptide fragment, comprising the N-terminal anticodon-binding domain of the lysyl tRNA synthetase encoded by the Escherichia coli LysS gene. The structure of LysN contains an OB-fold motif composed of a structurally conserved five-stranded beta-barrel capped by a poorly conserved alpha-helix between strands beta3 and beta4. Two additional alpha-helices, unique to the LysN structure, flank the N terminus of the OB-fold. Long range HNCO spectroscopy will be used to determine H-bonds in the protein LysN. The H-bond data will be used for structure determination/refinement.
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