The CcmC–CcmE interaction during cytochrome c maturation by System I is driven by protein–protein and not protein–heme contacts
Cytochromes c are ubiquitous proteins, essential for life in most organisms. Their distinctive characteristic is the covalent attachment of heme to their polypeptide chain. This post-translational modification is performed by a dedicated protein system, which in many Gram-negative bacteria and plant...
Main Authors: | Shevket, S, Gonzalez, D, Cartwright, J, Kleanthous, C, Ferguson, S, Redfield, C, Mavridou, D |
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Format: | Journal article |
Sprog: | English |
Udgivet: |
American Society for Biochemistry and Molecular Biology
2018
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Lignende værker
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NMR studies on holo-CcmE and in vivo mutagenesis studies on the interaction between CcmC and CcmE
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Functional characterization of the C-terminal domain of the cytochrome c maturation protein CcmE.
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c-Type cytochrome biogenesis can occur via a natural Ccm system lacking CcmH, CcmG, and the heme-binding histidine of CcmE.
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Complexation of CcmB with CcmACD safeguards heme translocation for cytochrome c maturation
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