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6I40

Crystal structure of murine neuroglobin bound to CO at 15K under illumination using optical fiber

Summary for 6I40
Entry DOI10.2210/pdb6i40/pdb
Related6I3T
DescriptorNeuroglobin, PROTOPORPHYRIN IX CONTAINING FE, CARBON MONOXIDE, ... (7 entities in total)
Functional Keywordsoxygen transport/storage, carbon monoxide, photodissociation, oxygen transport
Biological sourceMus musculus (Mouse)
Total number of polymer chains1
Total formula weight18098.12
Authors
Savino, C.,Montemiglio, L.C.,Ardiccioni, C.,Exertier, C.,Vallone, B. (deposition date: 2018-11-08, release date: 2019-09-11, Last modification date: 2024-01-24)
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 (1.9 Å)
Structure validation

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