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1CYI

CYTOCHROME C6

Summary for 1CYI
Entry DOI10.2210/pdb1cyi/pdb
DescriptorCYTOCHROME C6, CADMIUM ION, HEME C, ... (4 entities in total)
Functional Keywordsphotosynthesis, chlamydomonas, electron transport protein (cytochrome)
Biological sourceChlamydomonas reinhardtii
Cellular locationPlastid, chloroplast thylakoid lumen: P08197
Total number of polymer chains1
Total formula weight10879.14
Authors
Kerfeld, C.A.,Yeates, T.O. (deposition date: 1995-05-09, release date: 1996-01-29, Last modification date: 2024-10-30)
Primary citationKerfeld, C.A.,Anwar, H.P.,Interrante, R.,Merchant, S.,Yeates, T.O.
The structure of chloroplast cytochrome c6 at 1.9 A resolution: evidence for functional oligomerization.
J.Mol.Biol., 250:627-647, 1995
Cited by
PubMed Abstract: 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.
PubMed: 7623381
DOI: 10.1006/jmbi.1995.0404
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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