5MJD
metNgb under oxygen at 80 bar
Summary for 5MJD
Entry DOI | 10.2210/pdb5mjd/pdb |
Related | 4O4T 5MJC |
Descriptor | Neuroglobin, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (5 entities in total) |
Functional Keywords | oxygen complex storage cavity, transport protein |
Biological source | Mus musculus (House Mouse) |
Total number of polymer chains | 1 |
Total formula weight | 17379.42 |
Authors | Prange, T.,Colloc'h, N.,Carpentier, P. (deposition date: 2016-11-30, release date: 2017-12-20, Last modification date: 2024-01-17) |
Primary citation | Ardiccioni, C.,Arcovito, A.,Della Longa, S.,van der Linden, P.,Bourgeois, D.,Weik, M.,Montemiglio, L.C.,Savino, C.,Avella, G.,Exertier, C.,Carpentier, P.,Prange, T.,Brunori, M.,Colloc'h, N.,Vallone, B. Ligand pathways in neuroglobin revealed by low-temperature photodissociation and docking experiments. Iucrj, 6:832-842, 2019 Cited by PubMed Abstract: A combined biophysical approach was applied to map gas-docking sites within murine neuroglobin (Ngb), revealing snapshots of events that might govern activity and dynamics in this unique hexacoordinate globin, which is most likely to be involved in gas-sensing in the central nervous system and for which a precise mechanism of action remains to be elucidated. The application of UV-visible microspectroscopy , solution X-ray absorption near-edge spectroscopy and X-ray diffraction experiments at 15-40 K provided the structural characterization of an Ngb photolytic intermediate by cryo-trapping and allowed direct observation of the relocation of carbon monoxide within the distal heme pocket after photodissociation. Moreover, X-ray diffraction at 100 K under a high pressure of dioxygen, a physiological ligand of Ngb, unravelled the existence of a storage site for O in Ngb which coincides with Xe-III, a previously described docking site for xenon or krypton. Notably, no other secondary sites were observed under our experimental conditions. PubMed: 31576217DOI: 10.1107/S2052252519008157 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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