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NMR Structure of the Heme Chaperone CcmE Reveals a Novel Functional Motif
- Source :
-
Structure . Nov2002, Vol. 10 Issue 11, p1551. 7p. - Publication Year :
- 2002
-
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. [Copyright &y& Elsevier]
- Subjects :
- *NUCLEAR magnetic resonance
*MOLECULAR chaperones
*HEME
Subjects
Details
- Language :
- English
- ISSN :
- 09692126
- Volume :
- 10
- Issue :
- 11
- Database :
- Academic Search Index
- Journal :
- Structure
- Publication Type :
- Academic Journal
- Accession number :
- 8546749
- Full Text :
- https://doi.org/10.1016/S0969-2126(02)00885-7