The repeat domain of the type III effector protein PthA shows a TPR-like structure and undergoes conformational changes upon DNA interaction
Version of Record online: 16 SEP 2010
Copyright © 2010 Wiley-Liss, Inc.
Proteins: Structure, Function, and Bioinformatics
Volume 78, Issue 16, pages 3386–3395, December 2010
How to Cite
Murakami, M. T., Sforça, M. L., Neves, J. L., Paiva, J. H., Domingues, M. N., Pereira, A. L. A., de Mattos Zeri, A. C. and Benedetti, C. E. (2010), The repeat domain of the type III effector protein PthA shows a TPR-like structure and undergoes conformational changes upon DNA interaction. Proteins, 78: 3386–3395. doi: 10.1002/prot.22846
- Issue online: 8 NOV 2010
- Version of Record online: 16 SEP 2010
- Accepted manuscript online: 17 AUG 2010 12:00AM EST
- Manuscript Accepted: 24 JUL 2010
- Manuscript Revised: 16 JUL 2010
- Manuscript Received: 26 MAY 2010
- Fundação de Amparo à Pesquisa do Estado de São (FAPESP)
- Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Additional Supporting Information may be found in the online version of this article.
|PROT_22846_sm_SuppFig1.pdf||1440K||Supporting Information Figure 1. Correlation between the chemical shift index and the NOE connectivity. (a) Hα proton chemical shift index of the 1.5-repeat peptide. (b) Summary of NOEs are represented by the thickness of the lines and are classified as strong, medium and weak, corresponding to upper bound constraints of 2.5, 3.5, and 5.0 Å, respectively.|
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