1cc5
From Proteopedia
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|PDB= 1cc5 |SIZE=350|CAPTION= <scene name='initialview01'>1cc5</scene>, resolution 2.5Å | |PDB= 1cc5 |SIZE=350|CAPTION= <scene name='initialview01'>1cc5</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cc5 OCA], [http://www.ebi.ac.uk/pdbsum/1cc5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cc5 RCSB]</span> | ||
}} | }} | ||
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[[Category: Carter, D C.]] | [[Category: Carter, D C.]] | ||
[[Category: Stout, C D.]] | [[Category: Stout, C D.]] | ||
| - | [[Category: HEM]] | ||
[[Category: electron transport (heme protein)]] | [[Category: electron transport (heme protein)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:18:50 2008'' |
Revision as of 16:18, 30 March 2008
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| , resolution 2.5Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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