1dcd
From Proteopedia
(New page: 200px<br /><applet load="1dcd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dcd, resolution 2.00Å" /> '''DESULFOREDOXIN COMPL...) |
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| - | [[Image:1dcd.gif|left|200px]]<br /><applet load="1dcd" size=" | + | [[Image:1dcd.gif|left|200px]]<br /><applet load="1dcd" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dcd, resolution 2.00Å" /> | caption="1dcd, resolution 2.00Å" /> | ||
'''DESULFOREDOXIN COMPLEXED WITH CD2+'''<br /> | '''DESULFOREDOXIN COMPLEXED WITH CD2+'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Desulforedoxin (Dx), isolated from the sulfate reducing bacterium | + | Desulforedoxin (Dx), isolated from the sulfate reducing bacterium Desulfovibrio gigas, is a small homodimeric (2 x 36 amino acids) protein. Each subunit contains a high-spin iron atom tetrahedrally bound to four cysteinyl sulfur atoms, a metal center similar to that found in rubredoxin (Rd) type proteins. The simplicity of the active center in Dx and the possibility of replacing the iron by other metals make this protein an attractive case for the crystallographic analysis of metal-substituted derivatives. This study extends the relevance of Dx to the bioinorganic chemistry field and is important to obtain model compounds that can mimic the four sulfur coordination of metals in biology. Metal replacement experiments were carried out by reconstituting the apoprotein with In3+, Ga3+, Cd2+, Hg2+, and Ni2+ salts. The In3+ and Ga3+ derivatives are isomorphous with the iron native protein; whereas Cd2+, Hg2+, and Ni2+ substituted Dx crystallized under different experimental conditions, yielding two additional crystal morphologies; their structures were determined by the molecular replacement method. A comparison of the three-dimensional structures for all metal derivatives shows that the overall secondary and tertiary structures are maintained, while some differences in metal coordination geometry occur, namely, bond lengths and angles of the metal with the sulfur ligands. These data are discussed in terms of the entatic state theory. |
==About this Structure== | ==About this Structure== | ||
| - | 1DCD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_gigas Desulfovibrio gigas] with CD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1DCD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_gigas Desulfovibrio gigas] with <scene name='pdbligand=CD:'>CD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Archer, M.]] | [[Category: Archer, M.]] | ||
| - | [[Category: Carvalho, A | + | [[Category: Carvalho, A L.]] |
| - | [[Category: Romao, M | + | [[Category: Romao, M J.]] |
[[Category: Teixeira, S.]] | [[Category: Teixeira, S.]] | ||
[[Category: CD]] | [[Category: CD]] | ||
[[Category: rubredoxin type protein]] | [[Category: rubredoxin type protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:12 2008'' |
Revision as of 10:15, 21 February 2008
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DESULFOREDOXIN COMPLEXED WITH CD2+
Overview
Desulforedoxin (Dx), isolated from the sulfate reducing bacterium Desulfovibrio gigas, is a small homodimeric (2 x 36 amino acids) protein. Each subunit contains a high-spin iron atom tetrahedrally bound to four cysteinyl sulfur atoms, a metal center similar to that found in rubredoxin (Rd) type proteins. The simplicity of the active center in Dx and the possibility of replacing the iron by other metals make this protein an attractive case for the crystallographic analysis of metal-substituted derivatives. This study extends the relevance of Dx to the bioinorganic chemistry field and is important to obtain model compounds that can mimic the four sulfur coordination of metals in biology. Metal replacement experiments were carried out by reconstituting the apoprotein with In3+, Ga3+, Cd2+, Hg2+, and Ni2+ salts. The In3+ and Ga3+ derivatives are isomorphous with the iron native protein; whereas Cd2+, Hg2+, and Ni2+ substituted Dx crystallized under different experimental conditions, yielding two additional crystal morphologies; their structures were determined by the molecular replacement method. A comparison of the three-dimensional structures for all metal derivatives shows that the overall secondary and tertiary structures are maintained, while some differences in metal coordination geometry occur, namely, bond lengths and angles of the metal with the sulfur ligands. These data are discussed in terms of the entatic state theory.
About this Structure
1DCD is a Single protein structure of sequence from Desulfovibrio gigas with as ligand. Full crystallographic information is available from OCA.
Reference
Structural studies by X-ray diffraction on metal substituted desulforedoxin, a rubredoxin-type protein., Archer M, Carvalho AL, Teixeira S, Moura I, Moura JJ, Rusnak F, Romao MJ, Protein Sci. 1999 Jul;8(7):1536-45. PMID:10422844
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