2vry
From Proteopedia
(Difference between revisions)
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| - | == | + | ==Mouse Neuroglobin with heme iron in the reduced ferrous state== |
<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 [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2vry]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VRY FirstGlance]. <br> |
| - | </td></tr><tr><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><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> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q1f|1q1f]], [[1w92|1w92]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q1f|1q1f]], [[1w92|1w92]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vry OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vry RCSB], [http://www.ebi.ac.uk/pdbsum/2vry 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=2vry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vry OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vry RCSB], [http://www.ebi.ac.uk/pdbsum/2vry PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | ||
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| + | 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<ref>PMID:18406335</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
==See Also== | ==See Also== | ||
*[[Neuroglobin|Neuroglobin]] | *[[Neuroglobin|Neuroglobin]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Lk3 transgenic mice]] |
[[Category: Angelo, P D.]] | [[Category: Angelo, P D.]] | ||
[[Category: Arcovito, A.]] | [[Category: Arcovito, A.]] | ||
Revision as of 08:48, 22 October 2014
Mouse Neuroglobin with heme iron in the reduced ferrous state
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Categories: Lk3 transgenic mice | Angelo, P D. | Arcovito, A. | Brunori, M. | Longa, S Della. | Mancini, G. | Moschetti, T. | Vallone, B. | Ferrous | Globin fold | Heme | Heme protein | Iron | Metal- binding | Metal-binding | Neuroglobin | Oxygen storage-transport complex | Oxygen transport | Photoreduction | Transport
