1xbn
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(New page: 200px<br /><applet load="1xbn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xbn, resolution 2.50Å" /> '''Crystal structure of...)
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Revision as of 23:41, 24 November 2007
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Crystal structure of a bacterial nitric oxide sensor: an ortholog of mammalian soluble guanylate cyclase heme domain
Overview
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.
About this Structure
1XBN is a Single protein structure of sequence from Thermoanaerobacter tengcongensis with OXY and HEM as ligands. Full crystallographic information is available from OCA.
Reference
Femtomolar sensitivity of a NO sensor from Clostridium botulinum., Nioche P, Berka V, Vipond J, Minton N, Tsai AL, Raman CS, Science. 2004 Nov 26;306(5701):1550-3. Epub 2004 Oct 7. PMID:15472039
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