1CC5

CRYSTAL STRUCTURE OF AZOTOBACTER CYTOCHROME C5 AT 2.5 ANGSTROMS RESOLUTION

Summary for 1CC5

• Entry DOI: 10.2210/pdb1cc5/pdb
• Descriptor: CYTOCHROME C5, HEME C (2 entities in total)
• Functional Keywords: electron transport (heme protein)
• Biological source: Azotobacter vinelandii
• Total number of polymer chains: 1
• Total formula weight: 8808.75

Authors

Stout, C.D.,Carter, D.C. (deposition date: 1984-08-10, release date: 1984-10-29, Last modification date: 2026-09-30)

Primary citation

Carter, D.C.,Melis, K.A.,O'Donnell, S.E.,Burgess, B.K.,Furey Jr., W.R.,Wang, B.C.,Stout, C.D.
Crystal structure of Azotobacter cytochrome c5 at 2.5 A resolution.
J.Mol.Biol., 184:279-295, 1985

PubMed Abstract: The crystal structure of cytochrome c5 from Azotobacter vinelandii has been solved and refined to an R value of 0.29 at 2.5 A resolution. The structure of the oxidized protein was solved using a monoclinic crystal form. The structure was solved by multiple isomorphous replacements, re-fit to a solvent-leveled multiple isomorphous replacement map, and refined by restrained least squares. The structure reveals monomers associated about the crystallographic 2-fold axis by hydrophobic contacts at the "exposed heme edge". The overall conformation for the monomer is similar to that of Pseudomonas aeruginosa cytochrome c551. However, relative to a common heme conformation, c5 and c551 differ by an average of 6.8 A over 82 alpha-carbon positions and the propionates of c5 are much more exposed to solvent. The shortest heme--heme contact at the "dimer" interface is 6.3 A (Fe to Fe 16.4 A). Alignment of c5 and c551 shows that the two cytochromes, in spite of sequence differences, have remarkably similar charge distributions. A disulfide stacks on a tyrosine between the N- and C-terminal helices.

PubMed: 2993632
DOI: 10.1016/0022-2836(85)90380-8

Experimental method

X-RAY DIFFRACTION (2.5 Å)