1lm0

Solution structure and characterization of the heme chaperone CcmE

spinqualitylabelsall models 1lm0, 35 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1lm0 is a 1 chain structure with sequence from "pseudomonas_putrefaciens"_(derby_and_hammer)_long_and_hammer_1941 "pseudomonas putrefaciens" (derby and hammer) long and hammer 1941. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1j6q Gene: ccmE ("Pseudomonas putrefaciens" (Derby and Hammer) Long and Hammer 1941) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CCME_SHEON] 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 (By similarity). 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 covalent attachment of the heme cofactor in c-type cytochromes is a surprisingly complex process, which in bacteria involves a number of different proteins. Among the latter, the ccmE gene product is known to perform a key role in the heme delivery pathway in Gram-negative bacteria. The solution structure of the soluble domain of apo-CcmE from Shewanella putrefaciens was determined through NMR spectroscopy on a 13C,15N-labeled sample. The structure is characterized by a compact core with large regions of beta structure, while the N-terminal and C-terminal regions are essentially unstructured. The overall folding is similar to that of the so-called oligo-binding proteins (OB fold). Solvent-exposed aromatic residues, conserved in all CcmE homologues, have been found in the proximity of His131, the putative heme-binding residue, that could have a role in the interaction with heme. No interaction between CcmE and heme, as well as between CcmE and holocytochrome c, could be detected in vitro by electronic spectroscopy or by NMR. The data available suggest that the heme transfer process is likely to involve a heterooligomeric protein complex and occur under a tight enzymatic control. Solution structure and characterization of the heme chaperone CcmE.,Arnesano F, Banci L, Barker PD, Bertini I, Rosato A, Su XC, Viezzoli MS Biochemistry. 2002 Nov 19;41(46):13587-94. PMID:12427019 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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