4o2g

From Proteopedia

(Difference between revisions)

Revision as of 09:15, 5 August 2016

Crystal structure of carbomonoxy murine neuroglobin mutant V140W

Structural highlights

4o2g is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1w92, 4mu5, 4nzi, 4o1t, 4o35
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]

Publication Abstract from PubMed

Neuroglobin is a member of the globin family involved in neuroprotection; it is primarily expressed in the brain and retina of vertebrates. Neuroglobin belongs to the heterogeneous group of hexacoordinate globins that have evolved in animals, plants and bacteria, endowed with the capability of reversible intramolecular coordination, allowing the binding of small gaseous ligands (O2, NO and CO). In a unique fashion among haemoproteins, ligand-binding events in neuroglobin are dependent on the sliding of the haem itself within a preformed internal cavity, as revealed by the crystal structure of its CO-bound derivative. Point mutants of the neuroglobin internal cavity have been engineered and their functional and structural characterization shows that hindering the haem displacement leads to a decrease in CO affinity, whereas reducing the cavity volume without interfering with haem sliding has negligible functional effects.

Engineering the internal cavity of neuroglobin demonstrates the role of the haem-sliding mechanism.,Avella G, Ardiccioni C, Scaglione A, Moschetti T, Rondinelli C, Montemiglio LC, Savino C, Giuffre A, Brunori M, Vallone B Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1640-8. doi:, 10.1107/S1399004714007032. Epub 2014 May 29. PMID:24914975^[3]

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

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
↑ Avella G, Ardiccioni C, Scaglione A, Moschetti T, Rondinelli C, Montemiglio LC, Savino C, Giuffre A, Brunori M, Vallone B. Engineering the internal cavity of neuroglobin demonstrates the role of the haem-sliding mechanism. Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1640-8. doi:, 10.1107/S1399004714007032. Epub 2014 May 29. PMID:24914975 doi:http://dx.doi.org/10.1107/S1399004714007032

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4o2g"

@@ Line 1: / Line 1: @@
 ==Crystal structure of carbomonoxy murine neuroglobin mutant V140W==
 <StructureSection load='4o2g' size='340' side='right' caption='[[4o2g]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w92|1w92]], [[4mu5|4mu5]], [[4nzi|4nzi]], [[4o1t|4o1t]], [[4o35|4o35]]</td></tr>
-<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=4o2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o2g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o2g RCSB], [http://www.ebi.ac.uk/pdbsum/4o2g PDBsum]</span></td></tr>
+<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=4o2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o2g OCA], [http://pdbe.org/4o2g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o2g RCSB], [http://www.ebi.ac.uk/pdbsum/4o2g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o2g ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4o2g" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Neuroglobin|Neuroglobin]]
 == References ==
 <references/>

4o2g

From Proteopedia

Revision as of 09:15, 5 August 2016

Crystal structure of carbomonoxy murine neuroglobin mutant V140W

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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