1sr3
From Proteopedia
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Solution structure of the heme chaperone CcmE of Escherichia coli
Overview
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.
About this Structure
1SR3 is a Single protein structure of sequence from Escherichia coli. This structure superseeds the now removed PDB entry 1LIZ. Full crystallographic information is available from OCA.
Reference
NMR structure of the heme chaperone CcmE reveals a novel functional motif., Enggist E, Thony-Meyer L, Guntert P, Pervushin K, Structure. 2002 Nov;10(11):1551-7. PMID:12429096
Page seeded by OCA on Wed Nov 21 02:35:30 2007
