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Published Online October 7, 2004
Science DOI: 10.1126/science.1103596

Reports

Submitted on August 3, 2004
Accepted on September 27, 2004

Femtomolar Sensitivity of a NO Sensor from Clostridium botulinum

Pierre Nioche 1, Vladimir Berka 2, Julia Vipond 3, Nigel Minton 4, Ah-Lim Tsai 2, C. S. Raman 1*

1 Structural Biology Research Center and Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston, TX 77030, USA.
2 Division of Hematology, Internal Medicine, University of Texas Medical School, Houston, TX 77030, USA.
3 Health Protection Agency, Porton Down, Salisbury, Wiltshire SP4 0JG, UK.
4 Center of Biomolecular Sciences and Institute of Infection, Immunity and Inflammation, University of Nottingham, Nottingham NG7 2RD, UK.

* To whom correspondence should be addressed.
C. S. Raman , E-mail: c.s.raman{at}uth.tmc.edu

Nitric oxide (NO) is extremely toxic to Clostridium botulinum, but its molecular targets are unknown. Here, we identify a heme protein sensor (SONO) that displays femtomolar affinity for NO. The crystal structure of the SONO heme domain reveals a novel fold and a strategically placed tyrosine residue that modulates heme-nitrosyl coordination. Furthermore, the domain architecture of a SONO ortholog cloned from Chlamydomonas reinhardtii indicates that NO signaling through cyclic guanosine monophosphate arose before the origin of multicellular eukaryotes. Our findings have broad implications for understanding bacterial responses to NO, as well as for the activation of mammalian NO-sensitive guanylyl cyclase.


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