› 1lm0

Solution NMR

Solution structure and characterization of the heme chaperone CcmE

Released:
DOI: 10.2210/pdb1lm0/pdb
PDB entry 1lm0 coloured by chain, ensemble of 35 models, front view.
PDB entry 1lm0 coloured by chain, ensemble of 35 models, side view.
PDB entry 1lm0 coloured by chain, ensemble of 35 models, top view.
Source organism: Shewanella putrefaciens
Primary publication:
Solution structure and characterization of the heme chaperone CcmE.
Arnesano F, Banci L, Barker PD, Bertini I, Rosato A, Su XC, Viezzoli MS
Biochemistry 41 13587-94 (2002)
PMID: 12427019

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184420 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c-type biogenesis protein CcmE Chain: A
Molecule details ›
Chain: A
Length: 136 amino acids
Theoretical weight: 14.71 KDa
Source organism: Shewanella putrefaciens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8EK44 (Residues: 30-161; Coverage: 82%)
Gene names: SO_0259, ccmE, cycJ
Sequence domains: CcmE domain
Structure domains: Nucleic acid-binding proteins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this NMR entry.
Refinement method: simulated annealing, torsion angle dyanamics, restrained energy minimization
Expression system: Escherichia coli

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Citations

5 review citations

Cytochrome c biogenesis: mechanisms for covalent modifications and trafficking of heme and for heme-iron redox control.
Kranz et al. (2009)
4 more

2 mentions without citation

Protein Machineries Involved in the Attachment of Heme to Cytochrome c: Protein Structures and Molecular Mechanisms.
Travaglini-Allocatelli C. (2013)
1 more