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1yv1

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[[Image:1yv1.gif|left|200px]]<br /><applet load="1yv1" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1yv1.gif|left|200px]]
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caption="1yv1, resolution 1.50&Aring;" />
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'''Fully reduced state of nigerythrin (all ferrous)'''<br />
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{{Structure
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|PDB= 1yv1 |SIZE=350|CAPTION= <scene name='initialview01'>1yv1</scene>, resolution 1.50&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=FE2:FE (II) ION'>FE2</scene>
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|ACTIVITY=
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|GENE= ngr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=881 Desulfovibrio vulgaris])
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}}
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'''Fully reduced state of nigerythrin (all ferrous)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1YV1 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=FE2:'>FE2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YV1 OCA].
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1YV1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YV1 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15895271 15895271]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15895271 15895271]
[[Category: Desulfovibrio vulgaris]]
[[Category: Desulfovibrio vulgaris]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: rubrerythrin]]
[[Category: rubrerythrin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:09:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:27:50 2008''

Revision as of 13:27, 20 March 2008


PDB ID 1yv1

Drag the structure with the mouse to rotate
, resolution 1.50Å
Ligands:
Gene: ngr (Desulfovibrio vulgaris)
Coordinates: save as pdb, mmCIF, xml



Fully reduced state of nigerythrin (all ferrous)


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

1YV1 is a Single protein structure of sequence from Desulfovibrio vulgaris. 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

Page seeded by OCA on Thu Mar 20 15:27:50 2008

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