1i77

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(New page: 200px<br /><applet load="1i77" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i77, resolution 1.95&Aring;" /> '''CYTOCHROME C3 FROM D...)
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[[Image:1i77.gif|left|200px]]<br /><applet load="1i77" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1i77, resolution 1.95&Aring;" />
caption="1i77, resolution 1.95&Aring;" />
'''CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ESSEX 6'''<br />
'''CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ESSEX 6'''<br />
==Overview==
==Overview==
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Cytochrome c3, a small (14-kDa) soluble tetraheme protein was isolated, from the periplasmic fraction of Desulfovibrio desulfuricans strain Essex, 6. Its major physiological function appears to be that of an electron, carrier for the periplasmic hydrogenase. It has been also shown to, interact with the high-molecular-mass cytochrome complex in the, cytoplasmic membrane, which eventually feeds electrons into the, membraneous quinone pool, as well as with the membrane-associated, dissimilatory sulfite reductase. The EPR spectra show features of four, different low-spin Fe(III) hemes. Orthorhombic crystals of cytochrome c3, were obtained and X-ray diffraction data were collected to below 2 A, resolution. The structure was solved by molecular replacement using, cytochrome c3 from D. desulfuricans ATCC 27774 as a search model.
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Cytochrome c3, a small (14-kDa) soluble tetraheme protein was isolated from the periplasmic fraction of Desulfovibrio desulfuricans strain Essex 6. Its major physiological function appears to be that of an electron carrier for the periplasmic hydrogenase. It has been also shown to interact with the high-molecular-mass cytochrome complex in the cytoplasmic membrane, which eventually feeds electrons into the membraneous quinone pool, as well as with the membrane-associated dissimilatory sulfite reductase. The EPR spectra show features of four different low-spin Fe(III) hemes. Orthorhombic crystals of cytochrome c3 were obtained and X-ray diffraction data were collected to below 2 A resolution. The structure was solved by molecular replacement using cytochrome c3 from D. desulfuricans ATCC 27774 as a search model.
==About this Structure==
==About this Structure==
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1I77 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 HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I77 OCA].
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1I77 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=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I77 OCA].
==Reference==
==Reference==
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[[Category: Foerster, S.]]
[[Category: Foerster, S.]]
[[Category: Fritz, G.]]
[[Category: Fritz, G.]]
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[[Category: Kroneck, P.M.H.]]
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[[Category: Kroneck, P M.H.]]
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[[Category: Mann, K.H.]]
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[[Category: Mann, K H.]]
[[Category: Messerschmidt, A.]]
[[Category: Messerschmidt, A.]]
[[Category: HEM]]
[[Category: HEM]]
[[Category: multi-heme cytochrome c]]
[[Category: multi-heme cytochrome c]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:42:19 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:08:41 2008''

Revision as of 11:08, 21 February 2008


1i77, resolution 1.95Å

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CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ESSEX 6

Overview

Cytochrome c3, a small (14-kDa) soluble tetraheme protein was isolated from the periplasmic fraction of Desulfovibrio desulfuricans strain Essex 6. Its major physiological function appears to be that of an electron carrier for the periplasmic hydrogenase. It has been also shown to interact with the high-molecular-mass cytochrome complex in the cytoplasmic membrane, which eventually feeds electrons into the membraneous quinone pool, as well as with the membrane-associated dissimilatory sulfite reductase. The EPR spectra show features of four different low-spin Fe(III) hemes. Orthorhombic crystals of cytochrome c3 were obtained and X-ray diffraction data were collected to below 2 A resolution. The structure was solved by molecular replacement using cytochrome c3 from D. desulfuricans ATCC 27774 as a search model.

About this Structure

1I77 is a Single protein structure of sequence from Desulfovibrio desulfuricans with as ligand. Full crystallographic information is available from OCA.

Reference

Spectroscopic investigation and determination of reactivity and structure of the tetraheme cytochrome c3 from Desulfovibrio desulfuricans Essex 6., Einsle O, Foerster S, Mann K, Fritz G, Messerschmidt A, Kroneck PM, Eur J Biochem. 2001 May;268(10):3028-35. PMID:11358521

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