1cyi

<StructureSection load='1cyi' size='340' side='right' caption='[[1cyi]], [[Resolution|resolution]] 1.90&Aring;' scene=''>

<table><tr><td colspan='2'>[[1cyi]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CYI FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1cyi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cyi RCSB], [http://www.ebi.ac.uk/pdbsum/1cyi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cyi ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/CYC6_CHLRE CYC6_CHLRE]] Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cy/1cyi_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

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 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<ref>PMID:7623381</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1cyi" style="background-color:#fffaf0;"></div>

*[[Cytochrome c|Cytochrome c]]

[[Category: Kerfeld, C A]]

[[Category: Yeates, T O]]

[[Category: Chlamydomona]]

[[Category: Photosynthesis]]