1cgo
From Proteopedia
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|PDB= 1cgo |SIZE=350|CAPTION= <scene name='initialview01'>1cgo</scene>, resolution 1.8Å | |PDB= 1cgo |SIZE=350|CAPTION= <scene name='initialview01'>1cgo</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cgo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cgo OCA], [http://www.ebi.ac.uk/pdbsum/1cgo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cgo RCSB]</span> | ||
}} | }} | ||
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[[Category: Dobbs, A J.]] | [[Category: Dobbs, A J.]] | ||
[[Category: Faber, H R.]] | [[Category: Faber, H R.]] | ||
| - | [[Category: HEM]] | ||
[[Category: electron transport (cytochrome)]] | [[Category: electron transport (cytochrome)]] | ||
| - | ''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 19:21:26 2008'' |
Revision as of 16:21, 30 March 2008
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| , resolution 1.8Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CYTOCHROME C'
Overview
The three-dimensional structures of two cytochromes c' have been determined in order to analyse the common features of proteins of this family and their relationship with other four-helix bundle structures. The structure of cytochrome c' from Alcaligenes sp was determined by molecular replacement supplemented with the iron anomalous scattering and the use of a single isomorphous heavy-atom derivative, and was refined using synchrotron data to 1.8 A resolution. The final model, comprising 956 protein atoms (one monomer) and 89 water molecules, has a final R value of 0.188 for all data in the range 20.0-1.8 A resolution (14 673 reflections). The structure of the cytochrome c' from Alcaligenes denitrificans is isomorphous and essentially identical (r.m.s. deviation for all atoms 0.36 A). Although its amino-acid sequence has not been determined chemically, only four differences from that of Alcaligenes sp cytochrome c' were identified by the X-ray analysis. The final model for Alcaligenes denitrificans cytochrome c', comprising 953 protein atoms and 75 water molecules, gave a final R factor of 0.167 for all data in the range 20.0-2.15 A (8220 reflections). The cytochrome c' monomer forms a classic four-helix bundle, determined by the packing of hydrophobic side chains around the enclosed haem group. There are very few cross-linking hydrogen bonds between the helices, the principal side-chain hydrogen bonding involving one of the haem propionates and a conserved Arg residue. The cytochrome c' dimer is created by a crystallographic twofold axis. Monomer-monomer contacts primarily involve the two A helices, with size complementarity of side chains in a central solvent-excluded portion of the interface and hydrogen bonding at the periphery. Both species have a pyroglutamic acid N-terminal residue. The haem iron is five-coordinate, 0.32 A out of the haem plane towards the fifth ligand, His120. The unusual magnetic properties of the Fe atom may be linked to a conserved basic residue, Arg124, adjacent to His120.
About this Structure
1CGO is a Single protein structure of sequence from Alcaligenes sp.. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of cytochrome c' from two Alcaligenes species and the implications for four-helix bundle structures., Dobbs AJ, Anderson BF, Faber HR, Baker EN, Acta Crystallogr D Biol Crystallogr. 1996 Mar 1;52(Pt 2):356-68. PMID:15299707
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