Abstract
The H-NOX (Heme-nitric oxide/oxygen binding) domain is conserved across eukaryotes and bacteria. In human soluble guanylyl cyclase (sGC) the H-NOX domain functions as a sensor for the gaseous signaling agent nitric oxide (NO). sGC contains the heme-binding H-NOX domain at its N-terminus, which regulates the catalytic site contained within the C-terminal end of the enzyme catalyzing the conversion of GTP (guanosine 5′-triphosphate) to GMP (guanylyl monophosphate). Here, we present the backbone and side-chain assignments of the 1H, 13C and 15N resonances of the 183-residue H-NOX domain from Nostoc sp. through solution NMR.
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Abbreviations
- NMR:
-
Nuclear Magnetic Resonance
- HSQC:
-
Heteronuclear single quantum coherence
- H-NOX:
-
Heme–nitric oxide/oxygen binding domain
- sGC:
-
Soluble guanylyl cyclase
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"SEE-DRUG" Grant (EU FP7 REGPOT CT-2011-285950; www.seedrug.upatras.gr) is acknowledged for financial support.
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Ioannis I. Alexandropoulos and Aikaterini I. Argyriou have contributed equally to this work.
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Alexandropoulos, I.I., Argyriou, A.I., Marousis, K.D. et al. 1H, 13C, 15N backbone and side-chain resonance assignment of Nostoc sp. C139A variant of the heme–nitric oxide/oxygen binding (H-NOX) domain. Biomol NMR Assign 10, 395–400 (2016). https://doi.org/10.1007/s12104-016-9707-6
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DOI: https://doi.org/10.1007/s12104-016-9707-6