1h21
From Proteopedia
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| - | [[Image:1h21.jpg|left|200px]]<br /><applet load="1h21" size=" | + | [[Image:1h21.jpg|left|200px]]<br /><applet load="1h21" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1h21, resolution 2.50Å" /> | caption="1h21, resolution 2.50Å" /> | ||
'''A NOVEL IRON CENTRE IN THE SPLIT-SORET CYTOCHROME C FROM DESULFOVIBRIO DESULFURICANS ATCC 27774'''<br /> | '''A NOVEL IRON CENTRE IN THE SPLIT-SORET CYTOCHROME C FROM DESULFOVIBRIO DESULFURICANS ATCC 27774'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1H21 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_desulfuricans Desulfovibrio desulfuricans] with HEC as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1DDC. Known structural/functional Site: <scene name='pdbsite=AC1:Hec Binding Site For Chain D'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1H21 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_desulfuricans Desulfovibrio desulfuricans] with <scene name='pdbligand=HEC:'>HEC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1DDC. Known structural/functional Site: <scene name='pdbsite=AC1:Hec+Binding+Site+For+Chain+D'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H21 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: sulfate respiration]] | [[Category: sulfate respiration]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:45:20 2008'' |
Revision as of 07:45, 3 February 2008
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A NOVEL IRON CENTRE IN THE SPLIT-SORET CYTOCHROME C FROM DESULFOVIBRIO DESULFURICANS ATCC 27774
Overview
The facultative sulfate/nitrate-reducing bacterium Desulfovibrio, desulfuricans ATCC 27774 harbours a split-Soret cytochrome c. This, cytochrome is a homodimeric protein, having two bis-histidinyl c-type, haems per monomer. It has an unique architecture at the haem domain: each, haem has one of the coordinating histidines provided by the other monomer, and in each monomer the haems are parallel to each other, almost in van, der Waals contact. This work reports the cloning and sequencing of the, gene encoding for this cytochrome and shows, by transcriptional analysis, that it is more expressed in nitrate-grown cells than in sulfate-grown, ones. In addition, the gene-deduced amino acid sequence revealed two new, cysteine residues that could be involved in the binding of a non-haem iron, centre. Indeed, the presence of a novel type of an iron-sulfur centre, (possibly of the [2Fe-2S] type) was demonstrated by EPR spectroscopy, and, putative models for its localization and structure in the cytochrome, molecule are proposed on the basis of the so-far-known 3D crystallographic, structure of the aerobically purified split-Soret cytochrome, which lacks, this centre.
About this Structure
1H21 is a Single protein structure of sequence from Desulfovibrio desulfuricans with as ligand. This structure superseeds the now removed PDB entry 1DDC. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
A novel iron centre in the split-Soret cytochrome c from Desulfovibrio desulfuricans ATCC 27774., Abreu IA, Lourenco AI, Xavier AV, LeGall J, Coelho AV, Matias PM, Pinto DM, Armenia Carrondo M, Teixeira M, Saraiva LM, J Biol Inorg Chem. 2003 Feb;8(3):360-70. Epub 2002 Dec 19. PMID:12589573
Page seeded by OCA on Sun Feb 3 09:45:20 2008
Categories: Desulfovibrio desulfuricans | Single protein | Abreu, I.A. | Carrondo, M.A. | Coelho, A.V. | Legall, J. | Lourenco, A.I. | Matias, P.M. | Pinto, D.M. | Saraiva, L.M. | Teixeira, M. | Xavier, A.V. | HEC | Dimeric di-heme cytochrome | Electron transport | Novel fold | Novel iron-sulfur centre | Stacked heme arrangement | Sulfate respiration
