1cc5
From Proteopedia
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CRYSTAL STRUCTURE OF AZOTOBACTER CYTOCHROME C5 AT 2.5 ANGSTROMS RESOLUTION
Overview
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.
About this Structure
1CC5 is a Single protein structure of sequence from Azotobacter vinelandii with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of Azotobacter cytochrome c5 at 2.5 A resolution., Carter DC, Melis KA, O'Donnell SE, Burgess BK, Furey WR Jr, Wang BC, Stout CD, J Mol Biol. 1985 Jul 20;184(2):279-95. PMID:2993632
Page seeded by OCA on Thu Feb 21 12:04:34 2008
