1oj6

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Human brain neuroglobin three-dimensional structure

Structural highlights

1oj6 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.95Å
Ligands:HEM, SO4
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NGB_HUMAN 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] [3] [4] [5]

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, mainly expressed in vertebrate brain and retina, is a recently identified member of the globin superfamily. Augmenting O(2) supply, neuroglobin promotes survival of neurons upon hypoxic injury, potentially limiting brain damage. In the absence of exogenous ligands, neuroglobin displays a hexacoordinated heme. O(2) and CO bind to the heme iron, displacing the endogenous HisE7 heme distal ligand. Hexacoordinated human neuroglobin displays a classical globin fold adapted to host the reversible bis-histidyl heme complex and an elongated protein matrix cavity, held to facilitate O(2) diffusion to the heme. The neuroglobin structure suggests that the classical globin fold is endowed with striking adaptability, indicating that hemoglobin and myoglobin are just two examples within a wide and functionally diversified protein homology superfamily.

Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity.,Pesce A, Dewilde S, Nardini M, Moens L, Ascenzi P, Hankeln T, Burmester T, Bolognesi M Structure. 2003 Sep;11(9):1087-95. PMID:12962627[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
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See Also

References

  1. Burmester T, Weich B, Reinhardt S, Hankeln T. A vertebrate globin expressed in the brain. Nature. 2000 Sep 28;407(6803):520-3. PMID:11029004 doi:http://dx.doi.org/10.1038/35035093
  2. 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
  3. Watanabe S, Wakasugi K. Zebrafish neuroglobin is a cell-membrane-penetrating globin. Biochemistry. 2008 May 13;47(19):5266-70. doi: 10.1021/bi800286m. Epub 2008 Apr, 17. PMID:18416560 doi:http://dx.doi.org/10.1021/bi800286m
  4. Brittain T, Skommer J, Henty K, Birch N, Raychaudhuri S. A role for human neuroglobin in apoptosis. IUBMB Life. 2010 Dec;62(12):878-85. doi: 10.1002/iub.405. PMID:21190290 doi:http://dx.doi.org/10.1002/iub.405
  5. Tiso M, Tejero J, Basu S, Azarov I, Wang X, Simplaceanu V, Frizzell S, Jayaraman T, Geary L, Shapiro C, Ho C, Shiva S, Kim-Shapiro DB, Gladwin MT. Human neuroglobin functions as a redox-regulated nitrite reductase. J Biol Chem. 2011 May 20;286(20):18277-89. doi: 10.1074/jbc.M110.159541. Epub, 2011 Feb 4. PMID:21296891 doi:http://dx.doi.org/10.1074/jbc.M110.159541
  6. Pesce A, Dewilde S, Nardini M, Moens L, Ascenzi P, Hankeln T, Burmester T, Bolognesi M. Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity. Structure. 2003 Sep;11(9):1087-95. PMID:12962627

Contents


PDB ID 1oj6

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