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5MJD

metNgb under oxygen at 80 bar

Summary for 5MJD
Entry DOI10.2210/pdb5mjd/pdb
Related4O4T 5MJC
DescriptorNeuroglobin, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (5 entities in total)
Functional Keywordsoxygen complex storage cavity, transport protein
Biological sourceMus musculus (House Mouse)
Total number of polymer chains1
Total formula weight17379.42
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 citationArdiccioni, 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: 31576217
DOI: 10.1107/S2052252519008157
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

226707

數據於2024-10-30公開中

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