1XBN

Crystal structure of a bacterial nitric oxide sensor: an ortholog of mammalian soluble guanylate cyclase heme domain

Summary for 1XBN

• Entry DOI: 10.2210/pdb1xbn/pdb
• Descriptor: Methyl-accepting chemotaxis protein, OXYGEN MOLECULE, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• Functional Keywords: soluble guanylyl cyclase, nitric oxide, heme protein, cgmp, signaling protein
• Biological source: Thermoanaerobacter tengcongensis MB4
• Total number of polymer chains: 1
• Total formula weight: 23504.98

Authors

Nioche, P.,Raman, C.S. (deposition date: 2004-08-30, release date: 2004-09-07, Last modification date: 2024-02-14)

Primary citation

Nioche, P.,Berka, V.,Vipond, J.,Minton, N.,Tsai, A.-L.,Raman, C.S.
Femtomolar sensitivity of a NO sensor from Clostridium botulinum
Science, 306:1550-1553, 2004

PubMed Abstract: 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 previously undescribed 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.

PubMed: 15472039
DOI: 10.1126/science.1103596

Experimental method

X-RAY DIFFRACTION (2.5 Å)