NMR structure of the heme chaperone CcmE reveals a novel functional motif |
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Authors: | Enggist Elisabeth Thöny-Meyer Linda Güntert Peter Pervushin Konstantin |
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Affiliation: | 1. Institut für Mikrobiologie, Eidgenössische Technische Hochschule, CH-8092 Zürich, Switzerland;2. Laboratorium für Physikalische Chemie, Eidgenössische Technische Hochschule, CH-8092 Zürich, Switzerland;3. RIKEN Genomic Sciences Center, W505, 1-7-22 Suehiro, Tsurumi, Yokohama 230-0045, Japan |
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Abstract: | The concept of metal chaperones involves transient binding of metallic cofactors by specific proteins for delivery to enzymes in which they function. Metal chaperones thus provide a protective, as well as a transport, function. We report the first structure of a heme chaperone, CcmE, which comprises these two functions. We propose that the covalent attachment of heme to an exposed histidine occurs after heme binding at the surface of a rigid molecule with a flexible C-terminal domain. CcmE belongs to a family of proteins with a specific fold, which all share a function in delivery of specific molecular cargo. |
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