PMID:15513913
| Citation |
Ahuja, U and Thöny-Meyer, L (2005) CcmD is involved in complex formation between CcmC and the heme chaperone CcmE during cytochrome c maturation. J. Biol. Chem. 280:236-43 |
|---|---|
| Abstract |
CcmD is a small membrane protein involved in heme delivery to the heme chaperone CcmE during cytochrome c maturation. Here we show that it physically interacts with CcmE and CcmC, another essential component of the heme delivery system. We demonstrate the formation of a ternary complex consisting of CcmCDE. A deletion analysis of individual domains revealed that the central hydrophobic domain is essential for its function. Moreover, the C-terminal, cytoplasmic domain seems to require a net positive charge to be functional. Our topology analysis indicates that CcmD is an integral interfacial membrane protein with its N and C termini extruding into the cytoplasmic side of the membrane. Interactions of CcmD with either ferrochelatase, the last heme biosynthetic enzyme, or directly with heme were not detectable. We postulate a function for CcmD in protein-protein interaction or membrane protein assembly required for the heme delivery process. |
| Links |
PubMed Online version:10.1074/jbc.M410912200 |
| Keywords |
Amino Acid Sequence; Bacterial Outer Membrane Proteins/chemistry; Bacterial Outer Membrane Proteins/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Biological Transport; Cytochromes c/chemistry; Cytochromes c/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Heme/metabolism; Hemeproteins/chemistry; Hemeproteins/metabolism; Membrane Proteins/chemistry; Membrane Proteins/metabolism; Molecular Sequence Data; Protein Binding; Protein Conformation; Protein Structure, Tertiary |
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