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 /> In monoheme cytochromes ''c'', the other axial position may be left vacant or be occupied by histidine or methionine residues; however, it can sometimes be occupied by cysteine or leucine residues.<ref name=main />. In ''Rm''cyt''c'', '''XX represents a threonine (Thr46) and an alanine residue (Ala47); these two residues are not involved in coordinating the iron ligand.''' The typical monoheme cyt ''c'' fold is formed by helices <scene name='Sandbox_Reserved_335/Helices/2'>A, C, and E</scene>. ''Rm''cyt''c'' contains seven α-helices that are folded around the heme, 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>, and the disulfide linkages exist at ''~~'CysBLABLA~~ and ~~BLALBA''~~'.

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 /> In monoheme cytochromes ''c'', the other axial position may be left vacant or be occupied by histidine or methionine residues; however, it can sometimes be occupied by cysteine or leucine residues.<ref name=main />. In ''Rm''cyt''c'', '''XX represents a threonine (Thr46) and an alanine residue (Ala47); these two residues are not involved in coordinating the iron ligand.''' The typical monoheme cyt ''c'' fold is formed by helices <scene name='Sandbox_Reserved_335/Helices/2'>A, C, and E</scene>. ''Rm''cyt''c'' contains seven α-helices that are folded around the heme, 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>, and the disulfide linkages exist at <scene name='Sandbox_Reserved_335/Cys/1'>Cys45 and Cys48</scene>'.

Sandbox Reserved 335: Difference between revisions

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Revision as of 23:06, 3 April 2011 view source Melissa Morrison (talk \| contribs) 102 edits No edit summary ← Older edit		Revision as of 23:20, 3 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='Figure 2' scene='Sandbox_Reserved_335/Heme/1' />		<Structure load='3cp5' size='300' frame='true' align='right' caption='Figure 2' 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 /> In monoheme cytochromes ''c'', the other axial position may be left vacant or be occupied by histidine or methionine residues; however, it can sometimes be occupied by cysteine or leucine residues.<ref name=main />. In ''Rm''cyt''c'', '''XX represents a threonine (Thr46) and an alanine residue (Ala47); these two residues are not involved in coordinating the iron ligand.''' The typical monoheme cyt ''c'' fold is formed by helices <scene name='Sandbox_Reserved_335/Helices/2'>A, C, and E</scene>. ''Rm''cyt''c'' contains seven α-helices that are folded around the heme, 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>, and the disulfide linkages exist at ''~~'CysBLABLA~~ and ~~BLALBA''~~'.		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 /> In monoheme cytochromes ''c'', the other axial position may be left vacant or be occupied by histidine or methionine residues; however, it can sometimes be occupied by cysteine or leucine residues.<ref name=main />. In ''Rm''cyt''c'', '''XX represents a threonine (Thr46) and an alanine residue (Ala47); these two residues are not involved in coordinating the iron ligand.''' The typical monoheme cyt ''c'' fold is formed by helices <scene name='Sandbox_Reserved_335/Helices/2'>A, C, and E</scene>. ''Rm''cyt''c'' contains seven α-helices that are folded around the heme, 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>, and the disulfide linkages exist at <scene name='Sandbox_Reserved_335/Cys/1'>Cys45 and Cys48</scene>'.