5f0b: Difference between revisions

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'''Unreleased structure'''


The entry 5f0b is ON HOLD  until Paper Publication
==Crystal structure of murine neuroglobin mutant F106W at 280 MPa pressure==
 
<StructureSection load='5f0b' size='340' side='right' caption='[[5f0b]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
Authors: Colloc'h, N., Girard, E., Vallone, B., Prange, T.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5f0b]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F0B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F0B FirstGlance]. <br>
Description: Crystal structure of murine neuroglobin mutant F106W at 280 MPa 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">[[5eys|5eys]]</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=5f0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f0b OCA], [http://pdbe.org/5f0b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f0b RCSB], [http://www.ebi.ac.uk/pdbsum/5f0b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f0b 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 03:57, 20 October 2016

Crystal structure of murine neuroglobin mutant F106W at 280 MPa pressureCrystal structure of murine neuroglobin mutant F106W at 280 MPa pressure

Structural highlights

5f0b 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

5f0b, resolution 2.15Å

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