Certain enzymes that synthesize antibiotics play a game of pass the parcel, handing biosynthetic intermediates from one active site to another. A study reveals the dynamic nature of interactions between the enzyme domains.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
References
Frueh, D. P. et al. Nature 454, 903–906 (2008).
Koglin, A. et al. Nature 454, 907–911 (2008).
Tang, Y., Kim, C.-Y., Mathews, I. I., Cane, D. E. & Khosla, C. Proc. Natl Acad. Sci. USA 103, 11124–11129 (2006).
Tanovic, A. et al. Science 321, 659–663 (2008).
Jenni, S. et al. Science 316, 254–261 (2007).
Wolf-Watz, M. et al. Nature Struct. Mol. Biol. 11, 945–949 (2004).
Henzler-Wildman, K. A. et al. Nature 450, 913–916 (2007).
Koglin, A. et al. Science 312, 273–276 (2006).
Kumar, S. et al. Protein Sci. 9, 10–19 (2000).
Grünberg, R., Leckner, J. & Nilges, M. Structure 12, 2125–2136 (2004).
Khosla, C. et al. Annu. Rev. Biochem. 76, 195–221 (2007).
Lai, J. R., Koglin, A. & Walsh, C. T. Biochemistry 45, 14869–14879 (2006).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Kapur, S., Khosla, C. Fit for an enzyme. Nature 454, 832–833 (2008). https://doi.org/10.1038/454832a
Published:
Issue Date:
DOI: https://doi.org/10.1038/454832a