DOI: 10.1128/JB.00651-09
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History
- Published online July 13, 2009.
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Copyright © 2009 American Society for Microbiology
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- Accepted Manuscript version (May 29, 2009).
- You are viewing the most recent version of this article.
Author Information
- Ute Römling*
- Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, SE-171 77 Stockholm, Sweden
- ↵* Mailing address: Department of Microbiology, Tumor and Cell Biology, FE 280, Karolinska Institutet, SE-171 77 Stockholm, Sweden. Phone: 46-8-524 87319. Fax: 46-8-330744. E-mail: Ute.Romling{at}ki.se
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- Requirement for tight regulation of the c-di-GMP signal.
- Discovery of catalytically active and inactive EAL domains.
- Amino acids required for the PDE activity of EAL domains.
- Role of loop 6 in EAL domain activity.
- Loop 6 is involved in signal transduction.
- Restoration of loop 6 recovers the catalytic activity of an EAL domain.
- A classification scheme for EAL domains.
- A request for an EAL domain structure supporting suboptimal catalytic activity.
- Analysis of substrate binding specificity of EAL domains.
- Conclusions.
- ACKNOWLEDGMENTS
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