Sandbox Reserved 335: Difference between revisions

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== 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; most cytochromes ''c'' occur in a '''CXXCH motif~~'''~~, where a histidine residue is one of the two axial ligands of the heme iron.<ref name=main>PMID:18855424</ref><ref name=heme /> The other axial position, in monoheme cytochromes ''c'', may be left vacant or be occupied by histidine or methionine residues, but can sometimes be occupied by cysteine or leucine residues.<ref name=main />. The typical monoheme cyt ''c'' fold is formed by helices <scene name='Sandbox_Reserved_335/Helices/2'>A, C, and E</scene>. In ''Rm''cyt''c'' there are seven α-helices that are folded around the porphyrin ring, all connected by random coils.<ref name=main />

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; most cytochromes ''c'' occur in a <scene name='Sandbox_Reserved_335/Motif/1'>CXXCH motif</scene>, where a histidine residue is one of the two axial ligands of the heme iron.<ref name=main>PMID:18855424</ref><ref name=heme /> The other axial position, in monoheme cytochromes ''c'', may be left vacant or be occupied by histidine or methionine residues, but can sometimes be occupied by cysteine or leucine residues.<ref name=main />. The typical monoheme cyt ''c'' fold is formed by helices <scene name='Sandbox_Reserved_335/Helices/2'>A, C, and E</scene>. In ''Rm''cyt''c'' there are seven α-helices that are folded around the porphyrin ring, all connected by random coils.<ref name=main />

In ''Rm''cyt''c'', the porphyrin ring is axially coordinated by <scene name='Sandbox_Reserved_335/Axial/3'>His49 and Met100</scene>

Sandbox Reserved 335: Difference between revisions

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 == 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; most cytochromes ''c'' occur in a '''CXXCH motif''', where a histidine residue is one of the two axial ligands of the heme iron.<ref name=main>PMID:18855424</ref><ref name=heme /> The other axial position, in monoheme cytochromes ''c'', may be left vacant or be occupied by histidine or methionine residues, but can sometimes be occupied by cysteine or leucine residues.<ref name=main />. The typical monoheme cyt ''c'' fold is formed by helices <scene name='Sandbox_Reserved_335/Helices/2'>A, C, and E</scene>. In ''Rm''cyt''c'' there are seven α-helices that are folded around the porphyrin ring, all connected by random coils.<ref name=main />
+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; most cytochromes ''c'' occur in a <scene name='Sandbox_Reserved_335/Motif/1'>CXXCH motif</scene>, where a histidine residue is one of the two axial ligands of the heme iron.<ref name=main>PMID:18855424</ref><ref name=heme /> The other axial position, in monoheme cytochromes ''c'', may be left vacant or be occupied by histidine or methionine residues, but can sometimes be occupied by cysteine or leucine residues.<ref name=main />. The typical monoheme cyt ''c'' fold is formed by helices <scene name='Sandbox_Reserved_335/Helices/2'>A, C, and E</scene>. In ''Rm''cyt''c'' there are seven α-helices that are folded around the porphyrin ring, all connected by random coils.<ref name=main />
 In ''Rm''cyt''c'', the porphyrin ring is axially coordinated by <scene name='Sandbox_Reserved_335/Axial/3'>His49 and Met100</scene>