1ql3
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STRUCTURE OF THE SOLUBLE DOMAIN OF CYTOCHROME C552 FROM PARACOCCUS DENITRIFICANS IN THE REDUCED STATE
OverviewOverview
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 ... [(full description)]
About this StructureAbout this Structure
1QL3 is a [Single protein] structure of sequence from [Paracoccus denitrificans] with HEC as [ligand]. Structure known Active Sites: AHL, BHL, CHL and DHL. Full crystallographic information is available from [OCA].
ReferenceReference
Structure of the soluble domain of cytochrome c(552) from Paracoccus denitrificans in the oxidized and reduced states., Harrenga A, Reincke B, Ruterjans H, Ludwig B, Michel H, J Mol Biol. 2000 Jan 21;295(3):667-78. PMID:10623555
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