1cyi
From Proteopedia
(New page: 200px<br /><applet load="1cyi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cyi, resolution 1.9Å" /> '''CYTOCHROME C6'''<br /...) |
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| - | [[Image:1cyi.jpg|left|200px]]<br /><applet load="1cyi" size=" | + | [[Image:1cyi.jpg|left|200px]]<br /><applet load="1cyi" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cyi, resolution 1.9Å" /> | caption="1cyi, resolution 1.9Å" /> | ||
'''CYTOCHROME C6'''<br /> | '''CYTOCHROME C6'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The molecular structure of cytochrome c6 from the green alga Chlamydomonas | + | The molecular structure of cytochrome c6 from the green alga Chlamydomonas reinhardtii has been determined from two crystal forms and refined to 1.9 A resolution. The two crystal forms are likely the result of different levels of post-translational modification of the protein. This is the first report of a high-resolution structure of a chloroplast-derived class I c-type cytochrome. The overall fold is similar to that of other class I c-type cytochromes, consisting of a series of alpha-helices and turns that envelop the heme prosthetic group. There is also a short two-stranded anti-parallel beta-sheet in the vicinity of the methionine axial ligand to the heme; this region of the molecule is formed by the most highly conserved residues in c6-type cytochromes. Although class I c-type cytochromes are assumed to function as monomers, both crystal forms of cytochrome c6 exhibit oligomerization about the heme crevice that is, in part, mediated by the short anti-parallel beta-sheet. The functional significance of this oligomerization is supported by the appearance of similar interfaces in other electron transfer couples, HPLC and light-scattering data, and is furthermore consistent with kinetic data on electron transfer reactions of c6-type cytochromes. |
==About this Structure== | ==About this Structure== | ||
| - | 1CYI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii] with CD and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1CYI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii] with <scene name='pdbligand=CD:'>CD</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CYI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Chlamydomonas reinhardtii]] | [[Category: Chlamydomonas reinhardtii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Kerfeld, C | + | [[Category: Kerfeld, C A.]] |
| - | [[Category: Yeates, T | + | [[Category: Yeates, T O.]] |
[[Category: CD]] | [[Category: CD]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
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[[Category: photosynthesis]] | [[Category: photosynthesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:11:11 2008'' |
Revision as of 10:11, 21 February 2008
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CYTOCHROME C6
Overview
The molecular structure of cytochrome c6 from the green alga Chlamydomonas reinhardtii has been determined from two crystal forms and refined to 1.9 A resolution. The two crystal forms are likely the result of different levels of post-translational modification of the protein. This is the first report of a high-resolution structure of a chloroplast-derived class I c-type cytochrome. The overall fold is similar to that of other class I c-type cytochromes, consisting of a series of alpha-helices and turns that envelop the heme prosthetic group. There is also a short two-stranded anti-parallel beta-sheet in the vicinity of the methionine axial ligand to the heme; this region of the molecule is formed by the most highly conserved residues in c6-type cytochromes. Although class I c-type cytochromes are assumed to function as monomers, both crystal forms of cytochrome c6 exhibit oligomerization about the heme crevice that is, in part, mediated by the short anti-parallel beta-sheet. The functional significance of this oligomerization is supported by the appearance of similar interfaces in other electron transfer couples, HPLC and light-scattering data, and is furthermore consistent with kinetic data on electron transfer reactions of c6-type cytochromes.
About this Structure
1CYI is a Single protein structure of sequence from Chlamydomonas reinhardtii with and as ligands. Full crystallographic information is available from OCA.
Reference
The structure of chloroplast cytochrome c6 at 1.9 A resolution: evidence for functional oligomerization., Kerfeld CA, Anwar HP, Interrante R, Merchant S, Yeates TO, J Mol Biol. 1995 Jul 28;250(5):627-47. PMID:7623381
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