1ql3: Difference between revisions

The crystal structure of the soluble domain of the membrane bound, cytochrome c(552) (cytochrome c(552)') from Paracoccus denitrificans was, determined using the multiwavelength anomalous diffraction technique and, refined at 1.5 A resolution for the oxidized and at 1. 4 A for the reduced, state. This is the first high-resolution crystal structure of a cytochrome, c at low ionic strength in both redox states. The atomic model allowed for, a detailed assessment of the structural properties including the secondary, structure, the heme geometry and interactions, and the redox-coupled, structural changes. In general, the structure has the same features as, that of known eukaryotic cytochromes c. However, the surface properties, are very different. Cytochrome c(552)' has a large strongly negatively, charged surface part and a smaller positively charged area around the, solvent-exposed heme atoms. One of the internal water molecules conserved, in all structures of eukaryotic cytochromes c is also present in this, bacterial cytochrome c. It contributes to the interactions between the, side-chain of Arg36 and the heme propionate connected to pyrrole ring A., Reduction of the oxidized crystals does not influence the conformation of, cytochrome c(552)' in contrast to eukaryotic cytochromes c. The oxidized, cytochrome c(552)', especially the region of amino acid residues 40 to 56, appears to be more flexible than the reduced one.

1QL3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans] with HEC as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Sites: AHL, BHL, CHL and DHL. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QL3 OCA].  

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