|
|
| Line 3: |
Line 3: |
| | <StructureSection load='2vry' size='340' side='right'caption='[[2vry]], [[Resolution|resolution]] 1.87Å' scene=''> | | <StructureSection load='2vry' size='340' side='right'caption='[[2vry]], [[Resolution|resolution]] 1.87Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vry]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VRY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vry]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VRY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.87Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1q1f|1q1f]], [[1w92|1w92]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vry OCA], [https://pdbe.org/2vry PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vry RCSB], [https://www.ebi.ac.uk/pdbsum/2vry PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vry ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vry OCA], [https://pdbe.org/2vry PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vry RCSB], [https://www.ebi.ac.uk/pdbsum/2vry PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vry ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/NGB_MOUSE NGB_MOUSE] Involved in oxygen transport in the brain. Hexacoordinate globin, displaying competitive binding of oxygen or the distal His residue to the iron atom. Not capable of penetrating cell membranes. The deoxygenated form exhibits nitrite reductase activity inhibiting cellular respiration via NO-binding to cytochrome c oxidase. Involved in neuroprotection during oxidative stress. May exert its anti-apoptotic activity by acting to reset the trigger level of mitochondrial cytochrome c release necessary to commit the cells to apoptosis.<ref>PMID:11473111</ref> <ref>PMID:11473128</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 35: |
Line 37: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Angelo, P D]] | + | [[Category: Arcovito A]] |
| - | [[Category: Arcovito, A]] | + | [[Category: Brunori M]] |
| - | [[Category: Brunori, M]] | + | [[Category: D'Angelo P]] |
| - | [[Category: Longa, S Della]] | + | [[Category: Della Longa S]] |
| - | [[Category: Mancini, G]] | + | [[Category: Mancini G]] |
| - | [[Category: Moschetti, T]] | + | [[Category: Moschetti T]] |
| - | [[Category: Vallone, B]] | + | [[Category: Vallone B]] |
| - | [[Category: Ferrous]]
| + | |
| - | [[Category: Globin fold]]
| + | |
| - | [[Category: Heme]]
| + | |
| - | [[Category: Heme protein]]
| + | |
| - | [[Category: Iron]]
| + | |
| - | [[Category: Metal- binding]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Neuroglobin]]
| + | |
| - | [[Category: Oxygen storage-transport complex]]
| + | |
| - | [[Category: Oxygen transport]]
| + | |
| - | [[Category: Photoreduction]]
| + | |
| - | [[Category: Transport]]
| + | |
| Structural highlights
Function
NGB_MOUSE Involved in oxygen transport in the brain. Hexacoordinate globin, displaying competitive binding of oxygen or the distal His residue to the iron atom. Not capable of penetrating cell membranes. The deoxygenated form exhibits nitrite reductase activity inhibiting cellular respiration via NO-binding to cytochrome c oxidase. Involved in neuroprotection during oxidative stress. May exert its anti-apoptotic activity by acting to reset the trigger level of mitochondrial cytochrome c release necessary to commit the cells to apoptosis.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
An X-ray diffraction and X-ray absorption spectroscopy joint study of neuroglobin.,Arcovito A, Moschetti T, D'Angelo P, Mancini G, Vallone B, Brunori M, Della Longa S Arch Biochem Biophys. 2008 Jul 1;475(1):7-13. Epub 2008 Mar 29. PMID:18406335[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Couture M, Burmester T, Hankeln T, Rousseau DL. The heme environment of mouse neuroglobin. Evidence for the presence of two conformations of the heme pocket. J Biol Chem. 2001 Sep 28;276(39):36377-82. Epub 2001 Jul 25. PMID:11473111 doi:http://dx.doi.org/10.1074/jbc.M103907200
- ↑ Dewilde S, Kiger L, Burmester T, Hankeln T, Baudin-Creuza V, Aerts T, Marden MC, Caubergs R, Moens L. Biochemical characterization and ligand binding properties of neuroglobin, a novel member of the globin family. J Biol Chem. 2001 Oct 19;276(42):38949-55. Epub 2001 Jul 25. PMID:11473128 doi:http://dx.doi.org/10.1074/jbc.M106438200
- ↑ 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. 2008 Jul 1;475(1):7-13. Epub 2008 Mar 29. PMID:18406335 doi:10.1016/j.abb.2008.03.026
|
