1cc5: Difference between revisions

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[[Image:1cc5.gif|left|200px]]
{{Seed}}
[[Image:1cc5.png|left|200px]]


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{{STRUCTURE_1cc5|  PDB=1cc5  |  SCENE=  }}  
{{STRUCTURE_1cc5|  PDB=1cc5  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF AZOTOBACTER CYTOCHROME C5 AT 2.5 ANGSTROMS RESOLUTION'''
===CRYSTAL STRUCTURE OF AZOTOBACTER CYTOCHROME C5 AT 2.5 ANGSTROMS RESOLUTION===




==Overview==
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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.
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{{ABSTRACT_PUBMED_2993632}}


==About this Structure==
==About this Structure==
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[[Category: Carter, D C.]]
[[Category: Carter, D C.]]
[[Category: Stout, C D.]]
[[Category: Stout, C D.]]
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