BMB Reports

Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
권호 표지
DOI QR코드

DOI QR Code

Backbone 1H, 15N, and 13C Resonance Assignments of the Helicobacter pylori Acyl Carrier Protein

  • Park, Sung-Jean (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Kim, Ji-Sun (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Son, Woo-Sung (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Ahn, Hee-Chul (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Lee, Bong-Jin (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University)
  • Received : 2003.02.27
  • Accepted : 2003.03.17
  • Published : 2003.09.30
Download PDF
⟨ Previous Next ⟩

Abstract

One of the small proteins from Helicobacter pylori, acyl carrier protein (ACP), was investigated by NMR. ACP is related to various cellular processes, especially with the biosynthesis of fatty acid. The basic NMR resonance assignment is a prerequisite for the validation of a heterologuous protein interaction with ACP in H.pylori. Here, the results of the backbone $^1H$, $^{15}N$, and $^{l3}C$ resonance assignments of the H. pylori ACP are reported using double- and triple-resonance techniques. About 97% of all of the $^1HN$, $^{15}N$, $^{13}CO$, $^{13}C{\alpha}$, and $^{13}C{\beta}$ resonances that cover 76 of the 78 non-proline residues are clarified through sequential- and specific-assignments. In addition, four helical regions were clearly identified on the basis of the resonance assignments.

Keywords

References

  1. Ammar, Y. B., Matsabara, T., Ito, K., Iizuka, M., Limpasenti, T., Pongsawasdi, P. and Minamiura, N. (2002) New action pattern of a maltose-forming ${\alpha}-amylose$ from streptomyces sp. and its possible application in bakery. J. Biochem. Mol. Biol. 35, 568-575. https://doi.org/10.5483/BMBRep.2002.35.6.568
  2. Crump, M. P., Crosby, J., Dempsey, C. E., Parkinson, J. A., Murray, M., Hopwood, D. A. and Simpson, T. J. (1997) Solution structure of the actinorhodin polyketide synthase acyl carrier protein from Streptomyces coelicolor A3(2). Biochemistry 36, 6000-6008. https://doi.org/10.1021/bi970006+
  3. Holak, T. A., Nilges, M., Prestegard, J. H., Gronenborn, A. M. and Clore, G. M. (1988) Three-dimensional structure of acyl carrier protein in solution determined by nuclear magnetic resonance and the combined use of dynamical simulated annealing and distance geometry. Eur. J. Biochem. 175, 9-15. https://doi.org/10.1111/j.1432-1033.1988.tb14159.x
  4. Kim, Y. and Prestegard, J. H. (1989) A dynamic model for the structure of acyl carrier protein in solution. Biochemistry 28, 8792-8797. https://doi.org/10.1021/bi00448a017
  5. Kleinkauf, H. and Von Dohren, H. (1996) A nonribosomal system of peptide biosynthesis. Eur. J. Biochem. 236, 335-351. https://doi.org/10.1111/j.1432-1033.1996.00335.x
  6. Lynen, F. (1980) On the structure of fatty acid synthetase of yeast. Eur. J. Biochem. 112, 431-442.
  7. Park, J. E., Lee, K. -Y., Do, S. -I. and Lee, S. S. (2002) Expression and characterization of ${\bata}-1,4-galactosyltransferase$ from Neisseria meningitidis and Neisseria gonorrhoeae. J. Biochem. Mol. Biol. 35, 330-336. https://doi.org/10.5483/BMBRep.2002.35.3.330
  8. Parris, K. D., Lin, L., Tam, A., Mathew, R., Hixon, J., Stahl, M., Fritz, C. C., Seehra, J. and Somers, W. S. (2000) Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites. Structure 8, 883-895. https://doi.org/10.1016/S0969-2126(00)00178-7
  9. Sanyal, I., Lee, S. -L. and Flint, D. H. (1994) Biosynthesis of pimeloyl-CoA, a biotin precursor in Escherichia coli, follows a modified fatty acid synthesis pathway: $^{13}C-labeling$ studies. J. Am. Chem. Soc. 116, 2637-2638. https://doi.org/10.1021/ja00085a061
  10. Shen, B., Summers, R. G., Gramajo, H., Bibb, M. J. and Hutchinson, C. R. (1992) Purification and characterization of the acyl carrier protein of the Streptomyces glaucescens tetracenomycin C polyketide synthase. J. Bacteriol. 174, 3818-3821.
  11. Wishart, D. S. and Sykes, B. D. (1994) The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J. Biomol. NMR 4, 171-180.
  12. Wong, H. C., Liu, G., Zhang, Y. -M., Rock, C. O. and Zheng, J. (2002) The solution structure of acyl carrier protein from Mycobacterium tuberculosis. J. Biol. Chem. 277, 15874-15880. https://doi.org/10.1074/jbc.M112300200
  13. Xu, G. Y., Tam, A., Lin, L., Hixon, J., Fritz, C. C. and Powers, R. (2001) Solution structure of B. subtilis acyl carrier protein. Structure 9, 277-287. https://doi.org/10.1016/S0969-2126(01)00586-X