1cgo
From Proteopedia
(New page: 200px<br /><applet load="1cgo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cgo, resolution 1.8Å" /> '''CYTOCHROME C''''<br /...) |
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| - | [[Image:1cgo.jpg|left|200px]]<br /><applet load="1cgo" size=" | + | [[Image:1cgo.jpg|left|200px]]<br /><applet load="1cgo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cgo, resolution 1.8Å" /> | caption="1cgo, resolution 1.8Å" /> | ||
'''CYTOCHROME C''''<br /> | '''CYTOCHROME C''''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structures of two cytochromes c' have been | + | 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== | ==About this Structure== | ||
| - | 1CGO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Alcaligenes_sp. Alcaligenes sp.] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1CGO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Alcaligenes_sp. Alcaligenes sp.] 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=1CGO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Alcaligenes sp.]] | [[Category: Alcaligenes sp.]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Anderson, B | + | [[Category: Anderson, B F.]] |
| - | [[Category: Baker, E | + | [[Category: Baker, E N.]] |
| - | [[Category: Dobbs, A | + | [[Category: Dobbs, A J.]] |
| - | [[Category: Faber, H | + | [[Category: Faber, H R.]] |
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: electron transport (cytochrome)]] | [[Category: electron transport (cytochrome)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:05:55 2008'' |
Revision as of 10:05, 21 February 2008
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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. with as ligand. 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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