Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Originally published in Science Express on 17 November 2005
Science 9 December 2005:
Vol. 310. no. 5754, pp. 1658 - 1661
DOI: 10.1126/science.1120177
Prev | Table of Contents | Next

Reports

Evidence for Macromolecular Protein Rings in the Absence of Bulk Water

Brandon T. Ruotolo,1 Kevin Giles,2 Iain Campuzano,2 Alan M. Sandercock,1 Robert H. Bateman,2 Carol V. Robinson1*

We have examined the architecture of a protein complex in the absence of bulk water. By determining collision cross sections of assemblies of the trp RNA binding protein, TRAP, we established that the 11-membered ring topology of the complex can be maintained within a mass spectrometer. We also found that the binding of tryptophan enhances the stability of the ring structure and that addition of a specific RNA molecule increases the size of the complex and prevents structural collapse. These results provide definitive evidence that protein quaternary structure can be maintained in the absence of bulk water and highlight the potential of ion mobility separation for defining shapes of heterogeneous macromolecular assemblies.

1 Department of Chemistry, Lensfield Road, University of Cambridge, Cambridge CB2 1EW, UK.
2 Waters MS Technologies Centre, Manchester M55 5PP, UK.

* To whom correspondence should be addressed. E-mail: cvr24{at}cam.ac.uk

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
The structure of CrgA from Neisseria meningitidis reveals a new octameric assembly state for LysR transcriptional regulators.
S. Sainsbury, L. A. Lane, J. Ren, R. J. Gilbert, N. J. Saunders, C. V. Robinson, D. I. Stuart, and R. J. Owens (2009)
Nucleic Acids Res. 37, 4545-4558
   Abstract »    Full Text »    PDF »
Defining the Structural Basis of Human Plasminogen Binding by Streptococcal Surface Enolase.
A. J. Cork, S. Jergic, S. Hammerschmidt, B. Kobe, V. Pancholi, J. L. P. Benesch, C. V. Robinson, N. E. Dixon, J. A. Aquilina, and M. J. Walker (2009)
J. Biol. Chem. 284, 17129-17137
   Abstract »    Full Text »    PDF »
Pendular proteins in gases and new avenues for characterization of macromolecules by ion mobility spectrometry.
A. A. Shvartsburg, S. Y. Noskov, R. W. Purves, and R. D. Smith (2009)
PNAS 106, 6495-6500
   Abstract »    Full Text »    PDF »
Micelles Protect Membrane Complexes from Solution to Vacuum.
N. P. Barrera, N. Di Bartolo, P. J. Booth, and C. V. Robinson (2008)
Science 321, 243-246
   Abstract »    Full Text »    PDF »
Structural Insight into the Mechanism of Activation of the Toll Receptor by the Dimeric Ligand Spatzle.
M. Gangloff, A. Murali, J. Xiong, C. J. Arnot, A. N. Weber, A. M. Sandercock, C. V. Robinson, R. Sarisky, A. Holzenburg, C. Kao, et al. (2008)
J. Biol. Chem. 283, 14629-14635
   Abstract »    Full Text »    PDF »
Heterodimerization of CCR2 Chemokines and Regulation by Glycosaminoglycan Binding.
S. E. Crown, Y. Yu, M. D. Sweeney, J. A. Leary, and T. M. Handel (2006)
J. Biol. Chem. 281, 25438-25446
   Abstract »    Full Text »    PDF »
Detection Technologies. Ambient mass spectrometry..
R. G. Cooks, Z. Ouyang, Z. Takats, and J. M. Wiseman (2006)
Science 311, 1566-1570
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)