1cc5
From Proteopedia
(New page: 200px<br /><applet load="1cc5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cc5, resolution 2.5Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1cc5.gif|left|200px]]<br /><applet load="1cc5" size=" | + | [[Image:1cc5.gif|left|200px]]<br /><applet load="1cc5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cc5, resolution 2.5Å" /> | caption="1cc5, resolution 2.5Å" /> | ||
'''CRYSTAL STRUCTURE OF AZOTOBACTER CYTOCHROME C5 AT 2.5 ANGSTROMS RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF AZOTOBACTER CYTOCHROME C5 AT 2.5 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of cytochrome c5 from Azotobacter vinelandii has | + | 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== | ==About this Structure== | ||
| - | 1CC5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1CC5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CC5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Azotobacter vinelandii]] | [[Category: Azotobacter vinelandii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Carter, D | + | [[Category: Carter, D C.]] |
| - | [[Category: Stout, C | + | [[Category: Stout, C D.]] |
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: electron transport (heme protein)]] | [[Category: electron transport (heme protein)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:04:34 2008'' |
Revision as of 10:04, 21 February 2008
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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
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