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Article

The C-terminal flexible domain of the heme chaperone CcmE is important but not essential for its function.

Journal of bacteriology - 1 Jul 2003

Enggist Elisabeth, Thöny-Meyer Linda

Abstract excerpt

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...

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Identifiers

PMID: 12813076
DOI: 10.1128/JB.185.13.3821-3827.2003
PMCID: PMC161577

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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