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| [[Image:1cyi.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1cyi| PDB=1cyi | SCENE= }} | | {{STRUCTURE_1cyi| PDB=1cyi | SCENE= }} |
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| '''CYTOCHROME C6'''
| | ===CYTOCHROME C6=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_7623381}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 7623381 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_7623381}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Chlamydomona]] | | [[Category: Chlamydomona]] |
| [[Category: Photosynthesis]] | | [[Category: Photosynthesis]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:14:51 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:48:07 2008'' |
