Table of Contents
Journal of Crystallography
Volume 2016, Article ID 4504891, 6 pages
http://dx.doi.org/10.1155/2016/4504891
Research Article

The X-Ray Structure of the Ligand-Free Antibiotic Ristocetin-A Reveals the Role of the Monomer/Dimer Equilibrium in Its Binding Mode

Laboratoire de Cristallographie et RMN Biologiques, Faculté de Pharmacie, UMR 8015 CNRS, 4 avenue de l’Observatoire, 75006 Paris, France

Received 25 March 2016; Accepted 17 May 2016

Academic Editor: Rajesh G. Gonnade

Copyright © 2016 Thierry Prangé and William B. T. Cruse. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. V. Nahoum, S. Spector, and P. J. Loll, “Structure of ristocetin A in complex with a bacterial cell-wall mimetic,” Acta Crystallographica Section D: Biological Crystallography, vol. 65, no. 8, pp. 832–838, 2009. View at Publisher · View at Google Scholar · View at Scopus
  2. Y. Nitanai, T. Kikuchi, K. Kakoi, S. Hanamaki, I. Fujisawa, and K. Aoki, “Crystal structures of the complexes between vancomycin and cell-wall precursor analogs,” Journal of Molecular Biology, vol. 385, no. 5, pp. 1422–1432, 2009. View at Publisher · View at Google Scholar · View at Scopus
  3. C. Lehmann, G. Bunkóczi, L. Vértesy, and G. M. Sheldrick, “Structures of glycopeptide antibiotics with peptides that model bacterial cell-wall precursors,” Journal of Molecular Biology, vol. 318, no. 3, pp. 723–732, 2002. View at Publisher · View at Google Scholar · View at Scopus
  4. W. G. Prowse, “Conformation of a82846b, a glycopeptide antibiotic, complexed with its cell wall fragment: an asymmetric homodimer determined using nmr spectroscopy,” Biochemistry, vol. 34, no. 29, pp. 9632–9644, 1995. View at Publisher · View at Google Scholar · View at Scopus
  5. Y.-C. Liu, Y.-S. Li, S.-Y. Lyu et al., “Interception of teicoplanin oxidation intermediates yields new antimicrobial scaffolds,” Nature Chemical Biology, vol. 7, no. 5, pp. 304–309, 2011. View at Publisher · View at Google Scholar · View at Scopus
  6. N. J. Economou, V. Nahoum, S. D. Weeks et al., “A carrier protein strategy yields the structure of dalbavancin,” Journal of the American Chemical Society, vol. 134, no. 10, pp. 4637–4645, 2012. View at Publisher · View at Google Scholar · View at Scopus
  7. N. J. Economou, S. D. Weeks, K. C. Grasty et al., “Structure of the complex between teicoplanin and a bacterial cell-wall peptide: use of a carrier-protein approach,” Acta Crystallographica Section D, vol. 69, no. 4, pp. 520–533, 2013. View at Publisher · View at Google Scholar · View at Scopus
  8. Collaborative Computational Project 4, “The CCP4 suite: programs for protein crystallography,” Acta Crystallographica Section D, vol. 50, no. 5, pp. 760–763, 1994. View at Publisher · View at Google Scholar
  9. G. M. Sheldrick, “A short history of SHELX,” Acta Crystallographica Section A: Foundations of Crystallography, vol. 64, no. 1, pp. 112–122, 2007. View at Publisher · View at Google Scholar · View at Scopus
  10. I. Usón and G. M. Sheldrick, “Advances in direct methods for protein crystallography,” Current Opinion in Structural Biology, vol. 9, no. 5, pp. 643–648, 1999. View at Publisher · View at Google Scholar · View at Scopus
  11. G. M. Sheldrick, P. G. Jones, O. Kennard, D. H. Williams, and G. A. Smith, “Structure of vancomycin and its complex with acetyl-D-alanyl-D-alanine,” Nature, vol. 271, no. 5642, pp. 223–225, 1978. View at Publisher · View at Google Scholar · View at Scopus
  12. P. T. Beurskens, G. Beurskens, R. de Gelder, S. Garcia-Granda, R. O. Gould, and J. M. M. Smits, The DIRDIF2008 Program System, Crystallography Laboratory, University of Nijmegen, Nijmegen, Netherlands, 2008.
  13. W. L. DeLano, The PyMOL Molecular Graphics System, DeLano Scientific LLC, Palo Alto, Calif, USA, 2002.
  14. V. Nahoum, S. Spector, and P. J. Loll, “Erratum in Structure of ristocetin A in complex with a bacterial cell-wall mimetic,” Acta Crystallographica D: Biological Crystallography, vol. 67, part 6, p. 592, 2011. View at Google Scholar
  15. P. Groves, M. S. Searle, J. P. Mackay, and D. H. Williams, “The structure of an asymmetric dimer relevant to the mode of action of the glycopeptide antibiotics,” Structure, vol. 2, no. 8, pp. 747–754, 1994. View at Publisher · View at Google Scholar · View at Scopus
  16. Y. R. Cho, A. J. Maguire, A. C. Try, M. S. Westwell, P. Groves, and D. H. Williams, “Cooperativity and anti-cooperativity between ligand binding and the dimerization of ristocetin A: asymmetry of a homodimer complex and implications for signal transduction,” Chemistry and Biology, vol. 3, no. 3, pp. 207–215, 1996. View at Publisher · View at Google Scholar · View at Scopus