1cyi: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1cyi.jpg|left|200px]] | [[Image:1cyi.jpg|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1cyi", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
| | {{STRUCTURE_1cyi| PDB=1cyi | SCENE= }} | ||
| | |||
}} | |||
'''CYTOCHROME C6''' | '''CYTOCHROME C6''' | ||
| Line 27: | Line 24: | ||
[[Category: Kerfeld, C A.]] | [[Category: Kerfeld, C A.]] | ||
[[Category: Yeates, T O.]] | [[Category: Yeates, T O.]] | ||
[[Category: | [[Category: Chlamydomona]] | ||
[[Category: | [[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 | |||
Revision as of 10:14, 2 May 2008
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 Page seeded by OCA on Fri May 2 13:14:51 2008
