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Journal:JBIC:7
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| - | < | + | <StructureSection load="Cytc6.pdb" size="450" color="" frame="true" spin="on" Scene ="Journal:JBIC:7/Cv/2" side="right" caption="Cytochrome c6"> |
=== Structural and kinetic studies of imidazole binding to two members of the cytochrome c6 family reveal an important role for a conserved heme pocket residue === | === Structural and kinetic studies of imidazole binding to two members of the cytochrome c6 family reveal an important role for a conserved heme pocket residue === | ||
<big>Badri S. Rajagopal, Michael T. Wilson, Derek S. Bendall, Christopher J. Howe and Jonathan A.R. Worrall</big><ref>DOI 10.1007/s00775-011-0758-y</ref> | <big>Badri S. Rajagopal, Michael T. Wilson, Derek S. Bendall, Christopher J. Howe and Jonathan A.R. Worrall</big><ref>DOI 10.1007/s00775-011-0758-y</ref> | ||
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Protein (un)folding studies on cytochrome c have revealed that (un)folding involves structural units called 'foldons'. The regions in the Q51V imidazole-adduct where structural changes occur map well to the two foldons predicted to unfold first in cytochrome c. Thus <scene name='Journal:JBIC:7/Cv/14'>imidazole triggers the release of the methionine ligand in the Q51V variant</scene>, leading to the formation of an early unfolding intermediate that is stabilised by <scene name='Journal:JBIC:7/Cv/15'>imidazole binding to the vacant heme iron coordination position</scene>, enabling it to be captured in the crystalline form. | Protein (un)folding studies on cytochrome c have revealed that (un)folding involves structural units called 'foldons'. The regions in the Q51V imidazole-adduct where structural changes occur map well to the two foldons predicted to unfold first in cytochrome c. Thus <scene name='Journal:JBIC:7/Cv/14'>imidazole triggers the release of the methionine ligand in the Q51V variant</scene>, leading to the formation of an early unfolding intermediate that is stabilised by <scene name='Journal:JBIC:7/Cv/15'>imidazole binding to the vacant heme iron coordination position</scene>, enabling it to be captured in the crystalline form. | ||
| + | '''PDB reference:''' Structure of the imidazole-adduct of the ''Phormidium laminosum'' cytochrome c6 Q51V variant, [[3ph2]]. | ||
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| + | </StructureSection> | ||
<references/> | <references/> | ||
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- ↑ Rajagopal BS, Wilson MT, Bendall DS, Howe CJ, Worrall JA. Structural and kinetic studies of imidazole binding to two members of the cytochrome c (6) family reveal an important role for a conserved heme pocket residue. J Biol Inorg Chem. 2011 Jan 26. PMID:21267610 doi:10.1007/s00775-011-0758-y
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