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| - | [[Image:1dcd.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1dcd| PDB=1dcd | SCENE= }} | | {{STRUCTURE_1dcd| PDB=1dcd | SCENE= }} |
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| - | '''DESULFOREDOXIN COMPLEXED WITH CD2+'''
| + | ===DESULFOREDOXIN COMPLEXED WITH CD2+=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10422844}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10422844 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10422844}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Teixeira, S.]] | | [[Category: Teixeira, S.]] |
| | [[Category: Rubredoxin type protein]] | | [[Category: Rubredoxin type protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:41:17 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:48:58 2008'' |
Revision as of 19:49, 30 June 2008
Template:STRUCTURE 1dcd
DESULFOREDOXIN COMPLEXED WITH CD2+
Template:ABSTRACT PUBMED 10422844
About this Structure
1DCD is a Single protein structure of sequence from Desulfovibrio gigas. 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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