5eu2: Difference between revisions

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'''Unreleased structure'''


The entry 5eu2 is ON HOLD
==Crystal structure of murine neuroglobin mutant V101F at ambient pressure==
 
<StructureSection load='5eu2' size='340' side='right' caption='[[5eu2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
Authors: Colloc'h, N., Girard, E., Vallone, B., Prange, T.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5eu2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EU2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EU2 FirstGlance]. <br>
Description: Crystal structure of murine neuroglobin mutant V101F at ambient pressure
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5eet|5eet]]</td></tr>
[[Category: Colloc'H, N]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5eu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eu2 OCA], [http://pdbe.org/5eu2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eu2 RCSB], [http://www.ebi.ac.uk/pdbsum/5eu2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5eu2 ProSAT]</span></td></tr>
[[Category: Vallone, B]]
</table>
== Function ==
[[http://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> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Girard, E]]
[[Category: Girard, E]]
[[Category: Prange, T]]
[[Category: Prange, T]]
[[Category: Vallone, B]]
[[Category: H, N Colloc]]
[[Category: Globin]]
[[Category: Oxygen storage-transporter]]
[[Category: Transport protein]]

Revision as of 03:56, 20 October 2016

Crystal structure of murine neuroglobin mutant V101F at ambient pressureCrystal structure of murine neuroglobin mutant V101F at ambient pressure

Structural highlights

5eu2 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

References

  1. ↑ 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
  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

5eu2, resolution 2.00Å

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