Linked Life Data

12429096

Source:http://linkedlifedata.com/resource/pubmed/id/12429096

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2002-11-13
pubmed:abstractText
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.
pubmed:language
eng
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:author
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1551-7
pubmed:dateRevised
2006-11-15
pubmed:articleTitle
NMR structure of the heme chaperone CcmE reveals a novel functional motif.
pubmed:affiliation
Institut für Mikrobiologie, Eidgenössische Technische Hochschule, Zürich, Switzerland.