1cyi
From Proteopedia
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|PDB= 1cyi |SIZE=350|CAPTION= <scene name='initialview01'>1cyi</scene>, resolution 1.9Å | |PDB= 1cyi |SIZE=350|CAPTION= <scene name='initialview01'>1cyi</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> | + | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cyi OCA], [http://www.ebi.ac.uk/pdbsum/1cyi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cyi RCSB]</span> | ||
}} | }} | ||
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[[Category: Kerfeld, C A.]] | [[Category: Kerfeld, C A.]] | ||
[[Category: Yeates, T O.]] | [[Category: Yeates, T O.]] | ||
| - | [[Category: CD]] | ||
| - | [[Category: HEM]] | ||
[[Category: chlamydomona]] | [[Category: chlamydomona]] | ||
[[Category: photosynthesis]] | [[Category: photosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:31:00 2008'' |
Revision as of 16:31, 30 March 2008
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| , resolution 1.9Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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