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| [[Image:1cc5.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1cc5| PDB=1cc5 | SCENE= }} | | {{STRUCTURE_1cc5| PDB=1cc5 | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF AZOTOBACTER CYTOCHROME C5 AT 2.5 ANGSTROMS RESOLUTION'''
| | ===CRYSTAL STRUCTURE OF AZOTOBACTER CYTOCHROME C5 AT 2.5 ANGSTROMS RESOLUTION=== |
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| ==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. | | The line below this paragraph, {{ABSTRACT_PUBMED_2993632}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 2993632 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_2993632}} |
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| ==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.]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:34:22 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:32:26 2008'' |