1LM0

Solution structure and characterization of the heme chaperone CcmE

Summary for 1LM0

• Entry DOI: 10.2210/pdb1lm0/pdb
• Related: 1J6Q
• NMR Information: BMRB: 5407
• Descriptor: cytochrome c maturation protein E (1 entity in total)
• Functional Keywords: all-beta protein, heme delivery, cytochrome c maturation, ob-(oligonucleotide binding)fold, chaperone
• Biological source: Shewanella putrefaciens
• Total number of polymer chains: 1
• Total formula weight: 14714.40

Authors

Arnesano, F.,Banci, L.,Barker, P.D.,Bertini, I.,Rosato, A.,Su, X.C.,Viezzoli, M.S. (deposition date: 2002-04-30, release date: 2002-12-25, Last modification date: 2024-05-22)

Primary citation

Arnesano, F.,Banci, L.,Barker, P.D.,Bertini, I.,Rosato, A.,Su, X.C.,Viezzoli, M.S.
Solution structure and characterization of the heme chaperone CcmE
Biochemistry, 41:13587-13594, 2002

PubMed Abstract: 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.

PubMed: 12427019
DOI: 10.1021/bi026362w

Experimental method

SOLUTION NMR