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Structural Insight into H‐NOX Gas Sensing and Cognate Signaling Protein Regulation
Author(s) -
Guo Yirui,
Marletta Michael A.
Publication year - 2019
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800478
Subject(s) - nox , heme , biochemistry , chemistry , nitric oxide , signal transduction , chemotaxis , microbiology and biotechnology , ligand (biochemistry) , histidine kinase , signal transducing adaptor protein , histidine , biophysics , biology , receptor , enzyme , organic chemistry , combustion
Heme‐nitric oxide/oxygen binding (H‐NOX) proteins are a family of gas‐binding hemoproteins that bind diatomic gas ligands such as nitric oxide (NO) and oxygen (O 2 ). In bacteria, H‐NOXs are often associated with signaling partners, including histidine kinases (HKs), diguanylate cyclases (DGCs) or methyl‐accepting chemotaxis proteins (MCPs), either as a stand‐alone protein or as a domain of a larger polypeptide. H‐NOXs regulate the activity of cognate signaling proteins through ligand‐induced conformational changes in the H‐NOX domain and protein/protein interactions between the H‐NOX and the cognate signaling partner. This review summarizes recent progress toward deciphering the molecular mechanism of bacterial H‐NOX activation and the subsequent regulation of H‐NOX‐associated cognate sensor proteins from a structural and biochemical point of view.