1cyj: Difference between revisions

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   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cy/1cyj_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cy/1cyj_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cyj ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cyj ConSurf].
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<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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 1cyj" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 07:13, 9 October 2024

CYTOCHROME C6

1cyj, resolution 1.90Å

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