1cyi
From Proteopedia
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| - | [[Image:1cyi.jpg|left|200px]] | + | [[Image:1cyi.jpg|left|200px]] |
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| - | '''CYTOCHROME C6''' | + | {{Structure |
| + | |PDB= 1cyi |SIZE=350|CAPTION= <scene name='initialview01'>1cyi</scene>, resolution 1.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> and <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CYTOCHROME C6''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CYI is a [ | + | 1CYI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CYI OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7623381 7623381] |
[[Category: Chlamydomonas reinhardtii]] | [[Category: Chlamydomonas reinhardtii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: CD]] | [[Category: CD]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
| - | [[Category: | + | [[Category: chlamydomona]] |
[[Category: photosynthesis]] | [[Category: photosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:30:28 2008'' |
Revision as of 08:30, 20 March 2008
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| , resolution 1.9Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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