1cc5
From Proteopedia
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| - | [[Image:1cc5.gif|left|200px]] | + | [[Image:1cc5.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF AZOTOBACTER CYTOCHROME C5 AT 2.5 ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 1cc5 |SIZE=350|CAPTION= <scene name='initialview01'>1cc5</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF AZOTOBACTER CYTOCHROME C5 AT 2.5 ANGSTROMS RESOLUTION''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CC5 is a [ | + | 1CC5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CC5 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/2993632 2993632] |
[[Category: Azotobacter vinelandii]] | [[Category: Azotobacter vinelandii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: electron transport (heme protein)]] | [[Category: electron transport (heme protein)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:22:30 2008'' |
Revision as of 08:22, 20 March 2008
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| , resolution 2.5Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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