1yux
From Proteopedia
(New page: 200px<br /><applet load="1yux" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yux, resolution 1.60Å" /> '''Mixed valant state o...) |
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| - | [[Image:1yux.gif|left|200px]]<br /><applet load="1yux" size=" | + | [[Image:1yux.gif|left|200px]]<br /><applet load="1yux" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yux, resolution 1.60Å" /> | caption="1yux, resolution 1.60Å" /> | ||
'''Mixed valant state of nigerythrin'''<br /> | '''Mixed valant state of nigerythrin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | High-resolution crystal structures of Desulfovibrio vulgaris nigerythrin | + | High-resolution crystal structures of Desulfovibrio vulgaris nigerythrin (DvNgr), a member of the rubrerythrin (Rbr) family, demonstrate an approximately 2-A movement of one iron (Fe1) of the diiron site from a carboxylate to a histidine ligand upon conversion of the mixed-valent ([Fe2(II),Fe1(III)]) to diferrous states, even at cryogenic temperatures. This Glu<-->His ligand "toggling" of one iron, which also occurs in DvRbr, thus, appears to be a characteristic feature of Rbr-type diiron sites. Unique features of DvNgr revealed by these structures include redox-induced flipping of a peptide carbonyl that reversibly forms a hydrogen bond to the histidine ligand to Fe1 of the diiron site, an intra-subunit proximal orientation of the rubredoxin-(Rub)-like and diiron domains, and an electron transfer pathway consisting of six covalent and two hydrogen bonds connecting the Rub-like iron with Fe2 of the diiron site. This pathway can account for DvNgr's relatively rapid peroxidase turnover. The characteristic combination of iron sites together with the redox-dependent iron toggling between protein ligands can account for the selectivity of Rbrs for hydrogen peroxide over dioxygen. |
==About this Structure== | ==About this Structure== | ||
| - | 1YUX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris] with FE and FE2 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1YUX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris] with <scene name='pdbligand=FE:'>FE</scene> and <scene name='pdbligand=FE2:'>FE2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YUX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Desulfovibrio vulgaris]] | [[Category: Desulfovibrio vulgaris]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Iyer, R | + | [[Category: Iyer, R B.]] |
| - | [[Category: Kurtz, D | + | [[Category: Kurtz, D M.]] |
| - | [[Category: Lanzilotta, W | + | [[Category: Lanzilotta, W N.]] |
[[Category: Silaghi-Dumitrescu, R.]] | [[Category: Silaghi-Dumitrescu, R.]] | ||
[[Category: FE]] | [[Category: FE]] | ||
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[[Category: rubrythrin]] | [[Category: rubrythrin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:09:21 2008'' |
Revision as of 14:09, 21 February 2008
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Mixed valant state of nigerythrin
Overview
High-resolution crystal structures of Desulfovibrio vulgaris nigerythrin (DvNgr), a member of the rubrerythrin (Rbr) family, demonstrate an approximately 2-A movement of one iron (Fe1) of the diiron site from a carboxylate to a histidine ligand upon conversion of the mixed-valent ([Fe2(II),Fe1(III)]) to diferrous states, even at cryogenic temperatures. This Glu<-->His ligand "toggling" of one iron, which also occurs in DvRbr, thus, appears to be a characteristic feature of Rbr-type diiron sites. Unique features of DvNgr revealed by these structures include redox-induced flipping of a peptide carbonyl that reversibly forms a hydrogen bond to the histidine ligand to Fe1 of the diiron site, an intra-subunit proximal orientation of the rubredoxin-(Rub)-like and diiron domains, and an electron transfer pathway consisting of six covalent and two hydrogen bonds connecting the Rub-like iron with Fe2 of the diiron site. This pathway can account for DvNgr's relatively rapid peroxidase turnover. The characteristic combination of iron sites together with the redox-dependent iron toggling between protein ligands can account for the selectivity of Rbrs for hydrogen peroxide over dioxygen.
About this Structure
1YUX is a Single protein structure of sequence from Desulfovibrio vulgaris with and as ligands. Full crystallographic information is available from OCA.
Reference
High-resolution crystal structures of Desulfovibrio vulgaris (Hildenborough) nigerythrin: facile, redox-dependent iron movement, domain interface variability, and peroxidase activity in the rubrerythrins., Iyer RB, Silaghi-Dumitrescu R, Kurtz DM Jr, Lanzilotta WN, J Biol Inorg Chem. 2005 Jun;10(4):407-16. Epub 2005 May 14. PMID:15895271
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