PMID:12813076
| Citation |
Enggist, E and Thöny-Meyer, L (2003) The C-terminal flexible domain of the heme chaperone CcmE is important but not essential for its function. J. Bacteriol. 185:3821-7 |
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| Abstract |
CcmE is a heme chaperone active in the cytochrome c maturation pathway of Escherichia coli. It first binds heme covalently to strictly conserved histidine H130 and subsequently delivers it to apo-cytochrome c. The recently solved structure of soluble CcmE revealed a compact core consisting of a beta-barrel and a flexible C-terminal domain with a short alpha-helical turn. In order to elucidate the function of this poorly conserved domain, CcmE was truncated stepwise from the C terminus. Removal of all 29 amino acids up to crucial histidine 130 did not abolish heme binding completely. For detectable transfer of heme to type c cytochromes, only one additional residue, D131, was required, and for efficient cytochrome c maturation, the seven-residue sequence (131)DENYTPP(137) was required. When soluble forms of CcmE were expressed in the periplasm, the C-terminal domain had to be slightly longer to allow detection of holo-CcmE. Soluble full-length CcmE had low activity in cytochrome c maturation, indicating the importance of the N-terminal membrane anchor for the in vivo function of CcmE. |
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| Keywords |
Amino Acid Sequence; Apoenzymes; Bacterial Outer Membrane Proteins/chemistry; Bacterial Outer Membrane Proteins/genetics; Bacterial Outer Membrane Proteins/metabolism; Cell Membrane/metabolism; Cytochrome c Group/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Genes, Bacterial; Genetic Complementation Test; Heme/metabolism; Hemeproteins/chemistry; Hemeproteins/genetics; Hemeproteins/metabolism; Molecular Chaperones/metabolism; Molecular Sequence Data; Mutation; Periplasm/metabolism; Protein Structure, Tertiary; Sequence Alignment; Spectrum Analysis/methods |
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