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1H, 13C, and 15N NMR assignments of an engineered intein based on Mycobacterium tuberculosis RecA

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Abstract

The backbone and side chain resonance assignments of an engineered intein based on Mycobacterium tuberculosis RecA have been determined based on triple-resonance experiments with the uniformly [13C,15N]-labeled protein.

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References

  • Derbyshire V, Wood DW, et al (1997) Genetic definition of a protein-splicing domain: functional mini-inteins support structure predictions and a model for intein evolution. Proc Natl Acad Sci USA 94(21):11466–11471

    Article  ADS  Google Scholar 

  • Hiraga K, Derbyshire V, et al (2005) Minimization and stabilization of the Mycobacterium tuberculosis recA intein. J Mol Biol 354(4):916–926

    Article  Google Scholar 

  • Johnson MA, Southworth MW, et al (2007) NMR structure of a KlbA intein precursor from Methanococcus jannaschii. Protein Sci 16(7):1316–1328

    Article  Google Scholar 

  • Moure CM, Quiocho FA (2005) The structure and function of intein-associated homing endonucleases. Nucleic Acid Mol Biol 16(Homing Endonucleases and Inteins):257–271

    Article  Google Scholar 

  • Paulus H (2000) Protein splicing and related forms of protein autoprocessing. Annu Rev Biochem 69:447–496

    Article  Google Scholar 

  • Perler FB (2002) Inbase: the intein database. Nucleic Acids Res 30(1):383–384

    Article  Google Scholar 

  • Perler FB, Davis EO, et al (1994) Protein splicing elements: inteins and exteins—a definition of terms and recommended nomenclature. Nucleic Acids Res 22(7):1125–1127

    Article  Google Scholar 

  • Romanelli A, Shekhtman A, et al (2004) Semisynthesis of a segmental isotopically labeled protein splicing precursor: NMR evidence for an unusual peptide bond at the N-extein-intein junction. PNAS 101(17):6397–6402

    Article  ADS  Google Scholar 

  • Van Roey P, Pereira B, et al (2007) Crystallographic and mutational studies of mycobacterium tuberculosis recA mini-inteins suggest a pivotal role for a highly conserved aspartate residue. J Mol Biol 367(1):162–173

    Article  Google Scholar 

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Acknowledgement

The work was supported by NIH grants GM081408 (C.W.) and GM44844 (M.B.).

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Correspondence to Chunyu Wang.

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Du, Z., Liu, Y., Zheng, Y. et al. 1H, 13C, and 15N NMR assignments of an engineered intein based on Mycobacterium tuberculosis RecA. Biomol NMR Assign 2, 111–113 (2008). https://doi.org/10.1007/s12104-008-9098-4

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  • DOI: https://doi.org/10.1007/s12104-008-9098-4

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