2KII
NMR structure of the SO2144 H-NOX domain from Shewanella oneidensis in the Fe(II)CO ligation state
Summary for 2KII
| Entry DOI | 10.2210/pdb2kii/pdb |
| NMR Information | BMRB: 16276 |
| Descriptor | Putative uncharacterized protein, PROTOPORPHYRIN IX CONTAINING FE, CARBON MONOXIDE (3 entities in total) |
| Functional Keywords | h-nox, unknown function |
| Biological source | Shewanella oneidensis |
| Total number of polymer chains | 1 |
| Total formula weight | 21179.09 |
| Authors | Erbil, W.K. (deposition date: 2009-05-05, release date: 2009-11-17, Last modification date: 2024-05-22) |
| Primary citation | Erbil, W.K.,Price, M.S.,Wemmer, D.E.,Marletta, M.A. A structural basis for H-NOX signaling in Shewanella oneidensis by trapping a histidine kinase inhibitory conformation. Proc.Natl.Acad.Sci.USA, 106:19753-19760, 2009 Cited by PubMed Abstract: Heme nitric oxide/oxygen (H-NOX) proteins are found in eukaryotes where they are typically part of a larger protein such as soluble guanylate cyclase and in prokaryotes where they are often found in operons with a histidine kinase, suggesting that H-NOX proteins serve as sensors for NO and O(2) in signaling pathways. The Fe(II)-NO complex of the H-NOX protein from Shewanella oneidensis inhibits the autophosphorylation of the operon-associated histidine kinase, whereas the ligand-free H-NOX has no effect on the kinase. NMR spectroscopy was used to determine the structures of the Fe(II)-CO complex of the S. oneidensis H-NOX and the Fe(II)-CO complex of the H103G H-NOX mutant as a mimic of the ligand-free and kinase-inhibitory Fe(II)-NO H-NOX, respectively. The results provide a molecular glimpse into the ligand-induced conformational changes that may underlie kinase inhibition and the subsequent control of downstream signaling. PubMed: 19918063DOI: 10.1073/pnas.0911645106 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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