1sr3 | pdb_00001sr3

Solution structure of the heme chaperone CcmE of Escherichia coli

spinqualitylabelsall models 1sr3, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1sr3 is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. This structure supersedes the now removed PDB entry 1liz. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: CCME ("Bacillus coli" Migula 1895) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CCME_ECOLI] Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.[HAMAP-Rule:MF_01959] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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