1yv1
From Proteopedia
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|PDB= 1yv1 |SIZE=350|CAPTION= <scene name='initialview01'>1yv1</scene>, resolution 1.50Å | |PDB= 1yv1 |SIZE=350|CAPTION= <scene name='initialview01'>1yv1</scene>, resolution 1.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FE2:FE (II) ION'>FE2</scene> | + | |LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= ngr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=881 Desulfovibrio vulgaris]) | |GENE= ngr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=881 Desulfovibrio vulgaris]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1yux|1YUX]], [[1yuz|1YUZ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yv1 OCA], [http://www.ebi.ac.uk/pdbsum/1yv1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yv1 RCSB]</span> | ||
}} | }} | ||
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[[Category: Lanzilotta, W N.]] | [[Category: Lanzilotta, W N.]] | ||
[[Category: Silaghi-Dumitrescu, R.]] | [[Category: Silaghi-Dumitrescu, R.]] | ||
| - | [[Category: FE2]] | ||
[[Category: diiron center]] | [[Category: diiron center]] | ||
[[Category: electron transfer]] | [[Category: electron transfer]] | ||
| Line 34: | Line 36: | ||
[[Category: rubrerythrin]] | [[Category: rubrerythrin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:23:38 2008'' |
Revision as of 22:23, 30 March 2008
| |||||||
| , resolution 1.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | ngr (Desulfovibrio vulgaris) | ||||||
| Related: | 1YUX, 1YUZ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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