2VRY
Mouse Neuroglobin with heme iron in the reduced ferrous state
Summary for 2VRY
| Entry DOI | 10.2210/pdb2vry/pdb |
| Related | 1Q1F 1W92 |
| Descriptor | NEUROGLOBIN, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | oxygen storage-transport complex, metal- binding, photoreduction, oxygen transport, iron, heme, ferrous, transport, neuroglobin, globin fold, heme protein, metal-binding, oxygen storage/transport |
| Biological source | MUS MUSCULUS (MOUSE) |
| Total number of polymer chains | 1 |
| Total formula weight | 18115.19 |
| Authors | Arcovito, A.,Moschetti, T.,D'Angelo, P.,Mancini, G.,Vallone, B.,Brunori, M.,Della Longa, S. (deposition date: 2008-04-16, release date: 2008-05-06, Last modification date: 2023-12-13) |
| Primary citation | Arcovito, A.,Moschetti, T.,D'Angelo, P.,Mancini, G.,Vallone, B.,Brunori, M.,Della Longa, S. An X-Ray Diffraction and X-Ray Absorption Spectroscopy Joint Study of Neuroglobin. Arch.Biochem.Biophys., 475:7-, 2008 Cited by PubMed Abstract: Neuroglobin (Ngb) is a member of the globin family expressed in the vertebrate brain, involved in neuroprotection. A combined approach of X-ray diffraction (XRD) on single crystal and X-ray absorption spectroscopy (XAS) in solution, allows to determine the oxidation state and the structure of the Fe-heme both in the bis-histidine and the CO-bound (NgbCO) states. The overall data demonstrate that under X-ray the iron is photoreduced fairly rapidly, and that the previously reported X-ray structure of ferric Ngb [B. Vallone, K. Nienhaus, M. Brunori, G.U. Nienhaus, Proteins 56 (2004) 85-92] very likely refers to a photoreduced species indistinguishable from the dithionite reduced protein. Results from the XAS analysis of NgbCO in solution are in good agreement with XRD data on the crystal. However prolonged X-ray exposure at 15K determines CO release. This preliminary result paves the way to experiments aimed at the characterization of pentacoordinate ferrous Ngb, the only species competent in binding external ligands such as O2, CO or NO. PubMed: 18406335DOI: 10.1016/J.ABB.2008.03.026 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.87 Å) |
Structure validation
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