Sandbox Reserved 335: Difference between revisions

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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/3'>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 /> The heme group is axially coordinated by <scene name='Sandbox_Reserved_335/Axial/3'>His49 and Met100</scene>

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 /> The heme group 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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Revision as of 23:22, 1 April 2011 view source Melissa Morrison (talk \| contribs) 102 edits No edit summary ← Older edit		Revision as of 00:26, 2 April 2011 view source Melissa Morrison (talk \| contribs) 102 edits No edit summary Newer edit →
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	<Structure load='3cp5' size='300' frame='true' align='right' caption='Insert caption here' scene='Sandbox_Reserved_335/Heme/1' />		<Structure load='3cp5' size='300' frame='true' align='right' caption='Insert caption here' scene='Sandbox_Reserved_335/Heme/1' />

	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/3'>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 /> The heme group is axially coordinated by <scene name='Sandbox_Reserved_335/Axial/3'>His49 and Met100</scene>		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 /> The heme group is axially coordinated by <scene name='Sandbox_Reserved_335/Axial/3'>His49 and Met100</scene>