1jdl

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(New page: 200px<br /><applet load="1jdl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jdl, resolution 1.7&Aring;" /> '''Structure of cytochro...)
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[[Image:1jdl.jpg|left|200px]]<br /><applet load="1jdl" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jdl, resolution 1.7&Aring;" />
caption="1jdl, resolution 1.7&Aring;" />
'''Structure of cytochrome c2 from Rhodospirillum Centenum'''<br />
'''Structure of cytochrome c2 from Rhodospirillum Centenum'''<br />
==Overview==
==Overview==
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Cytochrome c(2) from the purple photosynthetic bacterium Rhodospirillum, centenum has been crystallized by the sitting-drop vapour-diffusion, method. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 29.7, b = 59.9, c = 65.4 A, and diffract to, a resolution limit of 1.7 A. The Fe-atom position was determined from its, anomalous scattering contribution and a molecular-replacement solution was, calculated. The correctness of the solution was confirmed by parallel, isomorphous replacement studies. The resulting model has a type I, cytochrome fold with two features, an extended alpha-helix and a, surface-charge distribution, that are distinctive to this protein. The, implications of these structural features for the ability of the, cytochrome to serve as an electron carrier are discussed.
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Cytochrome c(2) from the purple photosynthetic bacterium Rhodospirillum centenum has been crystallized by the sitting-drop vapour-diffusion method. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 29.7, b = 59.9, c = 65.4 A, and diffract to a resolution limit of 1.7 A. The Fe-atom position was determined from its anomalous scattering contribution and a molecular-replacement solution was calculated. The correctness of the solution was confirmed by parallel isomorphous replacement studies. The resulting model has a type I cytochrome fold with two features, an extended alpha-helix and a surface-charge distribution, that are distinctive to this protein. The implications of these structural features for the ability of the cytochrome to serve as an electron carrier are discussed.
==About this Structure==
==About this Structure==
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1JDL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodospirillum_centenum Rhodospirillum centenum] 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=1JDL OCA].
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1JDL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodospirillum_centenum Rhodospirillum centenum] 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=1JDL OCA].
==Reference==
==Reference==
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[[Category: Rhodospirillum centenum]]
[[Category: Rhodospirillum centenum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Allen, J.P.]]
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[[Category: Allen, J P.]]
[[Category: Camara-Artigas, A.]]
[[Category: Camara-Artigas, A.]]
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[[Category: Williams, J.C.]]
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[[Category: Williams, J C.]]
[[Category: HEM]]
[[Category: HEM]]
[[Category: alpha helix]]
[[Category: alpha helix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:08:28 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:27 2008''

Revision as of 11:21, 21 February 2008


1jdl, resolution 1.7Å

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Structure of cytochrome c2 from Rhodospirillum Centenum

Overview

Cytochrome c(2) from the purple photosynthetic bacterium Rhodospirillum centenum has been crystallized by the sitting-drop vapour-diffusion method. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 29.7, b = 59.9, c = 65.4 A, and diffract to a resolution limit of 1.7 A. The Fe-atom position was determined from its anomalous scattering contribution and a molecular-replacement solution was calculated. The correctness of the solution was confirmed by parallel isomorphous replacement studies. The resulting model has a type I cytochrome fold with two features, an extended alpha-helix and a surface-charge distribution, that are distinctive to this protein. The implications of these structural features for the ability of the cytochrome to serve as an electron carrier are discussed.

About this Structure

1JDL is a Single protein structure of sequence from Rhodospirillum centenum with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of cytochrome c2 from Rhodospirillum centenum., Camara-Artigas A, Williams JC, Allen JP, Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1498-505. Epub, 2001 Oct 25. PMID:11679712

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