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This Article ACCEPTED PREPRINT Full Text (PDF) All Versions of this Article: ps.036160.108v1 17/11/2015    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Google Scholar Articles by Rumpel, S. Articles by Zweckstetter, M. PubMed PubMed Citation Articles by Rumpel, S. Articles by Zweckstetter, M. Social Bookmarking                   What's this?

For the Record

Assignment-free solution NMR method reveals CesT as an unswapped homodimer

¹ Ontario Cancer Institute;
² Max Planck Institute for Biophysical Chemistry

(RECEIVED April 30, 2008; ACCEPTED July 24, 2008)

The X-ray structure of the homodimeric chaperone CesT is the only structure among the type three secretion system (TTSS) chaperones which shows a domain swap. This swap has potential importance for the mechanism of effector translocation through a TTSS. Here we present two NMR strategies exploiting preexisting structural models and residual dipolar couplings (RDCs), which reveal the unswapped 35.4 kDa dimer to be present in solution. Particularly efficient is the discrimination of a swapped and unswapped structural state performed simultaneously to automatic backbone assignment using only HN-RDCs and carbonyl backbone chemical shifts. This direct approach may prove to be generally useful to rapidly differentiate two structural models.

Keywords: Protein Structure/Folding; Conformational changes; Chaperonins; Structure; NMR Spectroscopy

³ E-mail: mzwecks{at}gwdg.de

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