Sandbox Reserved 335: Difference between revisions
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{{STRUCTURE_3cp5 | PDB=3cp5 | SCENE=Sandbox_reserved_335/Cyt_c/2}} | |||
'''Cytochrome ''c''''' (cyt ''c'') is a superfamily of proteins belonging to the class of [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] with a core of helices and a covalently-bound [http://en.wikipedia.org/wiki/Heme heme prosthetic group].<ref>SCOP http://scop.mrc-lmb.cam.ac.uk/scop-1.75/data/scop.b.b.i.b.html</ref><ref name=main /> The cytochrome ''c'' superfamily contains many different families including monodomain and multi-domain C-type cytochromes (ex. [http://proteopedia.org/wiki/index.php/1etp cyt c4], a two-domain C-type cytochrome, and [http://proteopedia.org/wiki/index.php/2ozy NrfB], a pentaheme C-type cytochrome). This page focuses mainly on the monoheme cytochrome ''c'', although other C-type cytochromes will be mentioned briefly. | |||
== Introduction == | |||
== Function == | |||
== Structure == | |||
All members in the C-type cytochrome superfamily contain a heme prosthetic group that is covalently attached to the protein via two thioether bonds to cysteine residues.<ref name=main>PMID:18855424</ref> Most cytochromes ''c'' occur in a CXXCH motif, where a histidine residue is one of the two axial ligands of the heme iron. The other axial position may be left vacant or be occupied mostly by histidine or methionine residues, but can sometimes be occupied by cysteine or leucine residues.<ref name=main /> | |||
== Mechanism == | |||
== Importance == | |||
== References == | |||
<references/> | |||
